Eriko Nango
Kyoto University
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Publication
Featured researches published by Eriko Nango.
Nature | 2017
Michihiro Suga; Fusamichi Akita; Michihiro Sugahara; Minoru Kubo; Yoshiki Nakajima; Takanori Nakane; Keitaro Yamashita; Yasufumi Umena; Makoto Nakabayashi; Takahiro Yamane; Takamitsu Nakano; Mamoru Suzuki; Tetsuya Masuda; Shigeyuki Inoue; Tetsunari Kimura; Takashi Nomura; Shinichiro Yonekura; Long Jiang Yu; Tomohiro Sakamoto; Taiki Motomura; Jinghua Chen; Yuki Kato; Takumi Noguchi; Kensuke Tono; Yasumasa Joti; Takashi Kameshima; Takaki Hatsui; Eriko Nango; Rie Tanaka; Hisashi Naitow
Photosystem II (PSII) is a huge membrane-protein complex consisting of 20 different subunits with a total molecular mass of 350 kDa for a monomer. It catalyses light-driven water oxidation at its catalytic centre, the oxygen-evolving complex (OEC). The structure of PSII has been analysed at 1.9 Å resolution by synchrotron radiation X-rays, which revealed that the OEC is a Mn4CaO5 cluster organized in an asymmetric, ‘distorted-chair’ form. This structure was further analysed with femtosecond X-ray free electron lasers (XFEL), providing the ‘radiation damage-free’ structure. The mechanism of O=O bond formation, however, remains obscure owing to the lack of intermediate-state structures. Here we describe the structural changes in PSII induced by two-flash illumination at room temperature at a resolution of 2.35 Å using time-resolved serial femtosecond crystallography with an XFEL provided by the SPring-8 ångström compact free-electron laser. An isomorphous difference Fourier map between the two-flash and dark-adapted states revealed two areas of apparent changes: around the QB/non-haem iron and the Mn4CaO5 cluster. The changes around the QB/non-haem iron region reflected the electron and proton transfers induced by the two-flash illumination. In the region around the OEC, a water molecule located 3.5 Å from the Mn4CaO5 cluster disappeared from the map upon two-flash illumination. This reduced the distance between another water molecule and the oxygen atom O4, suggesting that proton transfer also occurred. Importantly, the two-flash-minus-dark isomorphous difference Fourier map showed an apparent positive peak around O5, a unique μ4-oxo-bridge located in the quasi-centre of Mn1 and Mn4 (refs 4,5). This suggests the insertion of a new oxygen atom (O6) close to O5, providing an O=O distance of 1.5 Å between these two oxygen atoms. This provides a mechanism for the O=O bond formation consistent with that proposed previously.
Nature Methods | 2015
Michihiro Sugahara; Eiichi Mizohata; Eriko Nango; Mamoru Suzuki; Tomoyuki Tanaka; Tetsuya Masuda; Rie Tanaka; Tatsuro Shimamura; Yoshiki Tanaka; Chiyo Suno; Kentaro Ihara; Dongqing Pan; Keisuke Kakinouchi; Shigeru Sugiyama; Michio Murata; Tsuyoshi Inoue; Kensuke Tono; Changyong Song; Jaehyun Park; Takashi Kameshima; Takaki Hatsui; Yasumasa Joti; Makina Yabashi; So Iwata
Serial femtosecond X-ray crystallography (SFX) has revolutionized atomic-resolution structural investigation by expanding applicability to micrometer-sized protein crystals, even at room temperature, and by enabling dynamics studies. However, reliable crystal-carrying media for SFX are lacking. Here we introduce a grease-matrix carrier for protein microcrystals and obtain the structures of lysozyme, glucose isomerase, thaumatin and fatty acid–binding protein type 3 under ambient conditions at a resolution of or finer than 2 Å.
Science | 2016
Eriko Nango; Antoine Royant; Minoru Kubo; Takanori Nakane; Cecilia Wickstrand; Tetsunari Kimura; Tomoyuki Tanaka; Kensuke Tono; Changyong Song; Rie Tanaka; Toshi Arima; Ayumi Yamashita; Jun Kobayashi; Toshiaki Hosaka; Eiichi Mizohata; Przemyslaw Nogly; Michihiro Sugahara; Daewoong Nam; Takashi Nomura; Tatsuro Shimamura; Dohyun Im; Takaaki Fujiwara; Yasuaki Yamanaka; Byeonghyun Jeon; Tomohiro Nishizawa; Kazumasa Oda; Masahiro Fukuda; Rebecka Andersson; Petra Båth; Robert Dods
Snapshots of bacteriorhodopsin Bacteriorhodopsin is a membrane protein that harvests the energy content from light to transport protons out of the cell against a transmembrane potential. Nango et al. used timeresolved serial femtosecond crystallography at an x-ray free electron laser to provide 13 structural snapshots of the conformational changes that occur in the nanoseconds to milliseconds after photoactivation. These changes begin at the active site, propagate toward the extracellular side of the protein, and mediate internal protonation exchanges that achieve proton transport. Science, this issue p. 1552 Time-resolved serial crystallography using an x-ray free electron laser reveals structural changes in bacteriorhodopsin. Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds to milliseconds following photoactivation. An initially twisted retinal chromophore displaces a conserved tryptophan residue of transmembrane helix F on the cytoplasmic side of the protein while dislodging a key water molecule on the extracellular side. The resulting cascade of structural changes throughout the protein shows how motions are choreographed as bR transports protons uphill against a transmembrane concentration gradient.
Journal of Synchrotron Radiation | 2015
Kensuke Tono; Eriko Nango; Michihiro Sugahara; Changyong Song; Jaehyun Park; Tomoyuki Tanaka; Rie Tanaka; Yasumasa Joti; Takashi Kameshima; Shun Ono; Takaki Hatsui; Eiichi Mizohata; Mamoru Suzuki; Tatsuro Shimamura; Yoshiki Tanaka; So Iwata; Makina Yabashi
An experimental platform for serial femtosecond crystallography using an X-ray free-electron laser and its applications at SACLA are described.
Scientific Reports | 2015
Keitaro Yamashita; Dongqing Pan; Tomohiko Okuda; Michihiro Sugahara; Atsushi Kodan; Tomohiro Yamaguchi; Tomohiro Murai; Keiko Gomi; Naoki Kajiyama; Eiichi Mizohata; Mamoru Suzuki; Eriko Nango; Kensuke Tono; Yasumasa Joti; Takashi Kameshima; Jaehyun Park; Changyong Song; Takaki Hatsui; Makina Yabashi; So Iwata; Hiroaki Kato; Hideo Ago; Masaki Yamamoto; Toru Nakatsu
Serial femtosecond crystallography (SFX) with X-ray free electron lasers (XFELs) holds great potential for structure determination of challenging proteins that are not amenable to producing large well diffracting crystals. Efficient de novo phasing methods are highly demanding and as such most SFX structures have been determined by molecular replacement methods. Here we employed single isomorphous replacement with anomalous scattering (SIRAS) for phasing and demonstrate successful application to SFX de novo phasing. Only about 20,000 patterns in total were needed for SIRAS phasing while single wavelength anomalous dispersion (SAD) phasing was unsuccessful with more than 80,000 patterns of derivative crystals. We employed high energy X-rays from SACLA (12.6 keV) to take advantage of the large anomalous enhancement near the LIII absorption edge of Hg, which is one of the most widely used heavy atoms for phasing in conventional protein crystallography. Hard XFEL is of benefit for de novo phasing in the use of routinely used heavy atoms and high resolution data collection.
Proceedings of the National Academy of Sciences of the United States of America | 2016
Yohta Fukuda; Ka Man Tse; Takanori Nakane; Toru Nakatsu; Mamoru Suzuki; Michihiro Sugahara; Shigeyuki Inoue; Tetsuya Masuda; Fumiaki Yumoto; Naohiro Matsugaki; Eriko Nango; Kensuke Tono; Yasumasa Joti; Takashi Kameshima; Changyong Song; Takaki Hatsui; Makina Yabashi; Osamu Nureki; Michael E. P. Murphy; Tsuyoshi Inoue; So Iwata; Eiichi Mizohata
Significance Copper nitrite reductase (CuNiR) is involved in denitrification of the nitrogen cycle. Synchrotron X-rays rapidly reduce copper sites and decompose the substrate complex structure, which has made crystallographic studies of CuNiR difficult. Using femtosecond X-ray free electron lasers, we determined intact structures of CuNiR with and without nitrite. Based on the obtained structures, we proposed a redox-coupled proton switch model, which provides an explanation for proton-coupled electron transfer (PCET) in CuNiR. PCET is widely distributed through biogenic processes including respiratory and photosynthetic systems and is highly expected to be incorporated into bioinspired molecular devices. Our study also establishes the foundation for future studies on PCET in other systems. Proton-coupled electron transfer (PCET), a ubiquitous phenomenon in biological systems, plays an essential role in copper nitrite reductase (CuNiR), the key metalloenzyme in microbial denitrification of the global nitrogen cycle. Analyses of the nitrite reduction mechanism in CuNiR with conventional synchrotron radiation crystallography (SRX) have been faced with difficulties, because X-ray photoreduction changes the native structures of metal centers and the enzyme–substrate complex. Using serial femtosecond crystallography (SFX), we determined the intact structures of CuNiR in the resting state and the nitrite complex (NC) state at 2.03- and 1.60-Å resolution, respectively. Furthermore, the SRX NC structure representing a transient state in the catalytic cycle was determined at 1.30-Å resolution. Comparison between SRX and SFX structures revealed that photoreduction changes the coordination manner of the substrate and that catalytically important His255 can switch hydrogen bond partners between the backbone carbonyl oxygen of nearby Glu279 and the side-chain hydroxyl group of Thr280. These findings, which SRX has failed to uncover, propose a redox-coupled proton switch for PCET. This concept can explain how proton transfer to the substrate is involved in intramolecular electron transfer and why substrate binding accelerates PCET. Our study demonstrates the potential of SFX as a powerful tool to study redox processes in metalloenzymes.
Tetrahedron Letters | 2000
Katsumi Kakinuma; Eriko Nango; Fumitaka Kudo; Yoshitaka Matsushima; Tadashi Eguchi
Abstract A potential two-step process to catechol from d -glucose comprising one-pot incubation of d -glucose with recombinant 2-deoxy- scyllo -inosose synthase (BtrC) and hexokinase, together with chemical reductive dehydration of the resulting 2-deoxy- scyllo -inosose with HI, was developed.
Journal of Applied Crystallography | 2016
Takanori Nakane; Yasumasa Joti; Kensuke Tono; Makina Yabashi; Eriko Nango; So Iwata; Ryuichiro Ishitani; Osamu Nureki
A data processing pipeline for SACLA was developed, based on Cheetah and CrystFEL. Real-time analysis and rapid structure solution were enabled.
Acta Crystallographica Section D-biological Crystallography | 2015
Takanori Nakane; Changyong Song; Mamoru Suzuki; Eriko Nango; Jun Kobayashi; Tetsuya Masuda; Shigeyuki Inoue; Eiichi Mizohata; Toru Nakatsu; Tomoyuki Tanaka; Rie Tanaka; Tatsuro Shimamura; Kensuke Tono; Yasumasa Joti; Takashi Kameshima; Takaki Hatsui; Makina Yabashi; Osamu Nureki; So Iwata; Michihiro Sugahara
Sulfur SAD phasing facilitates the structure determination of diverse native proteins using femtosecond X-rays from free-electron lasers via serial femtosecond crystallography.
Philosophical Transactions of the Royal Society B | 2014
François-Xavier Gallat; Naohiro Matsugaki; Nathan P. Coussens; Koichiro J. Yagi; Marion Boudes; Tetsuya Higashi; Daisuke Tsuji; Yutaka Tatano; Mamoru Suzuki; Eiichi Mizohata; Kensuke Tono; Yasumasa Joti; Takashi Kameshima; Jaehyun Park; Changyong Song; Takaki Hatsui; Makina Yabashi; Eriko Nango; Kohji Itoh; Fasséli Coulibaly; Stephen S. Tobe; S. Ramaswamy; Barbara Stay; So Iwata; Leonard M. G. Chavas
The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography.