David J. Schuller
University of California, San Francisco
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Featured researches published by David J. Schuller.
Nature Structural & Molecular Biology | 1999
David J. Schuller; Angela Wilks; Paul R. Ortiz de Montellano; Thomas L. Poulos
Heme oxygenase catalyzes the first step in the oxidative degradation of heme. The crystal structure of heme oxygenase-1 (HO-1) reported here reveals a novel helical fold with the heme sandwiched between two helices. The proximal helix provides a heme iron ligand, His 25. Conserved glycines in the distal helix near the oxygen binding site allow close contact between the helix backbone and heme in addition to providing flexibility for substrate binding and product release. Regioselective oxygenation of the α-meso heme carbon is due primarily to steric influence of the distal helix.
Nature Structural & Molecular Biology | 2000
William N. Lanzilotta; David J. Schuller; Marc V. Thorsteinsson; Robert L. Kerby; Gary P. Roberts; Thomas L. Poulos
CooA is a homodimeric transcription factor that belongs to the catabolite activator protein (CAP) family. Binding of CO to the heme groups of CooA leads to the transcription of genes involved in CO oxidation in Rhodospirillum rubrum. The 2.6 Å structure of reduced (Fe2+) CooA reveals that His 77 in both subunits provides one heme ligand while the N-terminal nitrogen of Pro 2 from the opposite subunit provides the other ligand. A structural comparison of CooA in the absence of effector and DNA (off state) with that of CAP in the effector and DNA bound state (on state) leads to a plausible model for the mechanism of allosteric control in this class of proteins as well as the CO dependent activation of CooA.
Journal of Biological Chemistry | 2000
Jason Yano; Laura S. Koo; David J. Schuller; Huiying Li; Paul R. Ortiz de Montellano; Thomas L. Poulos
The structure of the first P450 identified in Archaea, CYP119 from Sulfolobus solfataricus, has been solved in two different crystal forms that differ by the ligand (imidazole or 4-phenylimidazole) coordinated to the heme iron. A comparison of the two structures reveals an unprecedented rearrangement of the active site to adapt to the different size and shape of ligands bound to the heme iron. These changes involve unraveling of the F helix C-terminal segment to extend a loop structure connecting the F and G helices, allowing the longer loop to dip down into the active site and interact with the smaller imidazole ligand. A comparison of CYP119 with P450cam and P450eryF indicates an extensive clustering of aromatic residues may provide the structural basis for the enhanced thermal stability of CYP119. An additional feature of the 4-phenylimidazole-bound structure is a zinc ion tetrahedrally bound by symmetry-related His and Glu residues.
Journal of Biological Chemistry | 2000
Yi Liu; Luke Koenigs Lightning; Hong Wei Huang; Pierre Moënne-Loccoz; David J. Schuller; Thomas L. Poulos; Thomas M. Loehr; Paul R. Ortiz de Montellano
The human heme oxygenase-1 crystal structure suggests that Gly-139 and Gly-143 interact directly with iron-bound ligands. We have mutated Gly-139 to an alanine, leucine, phenylalanine, tryptophan, histidine, or aspartate, and Gly-143 to a leucine, lysine, histidine, or aspartate. All of these mutants bind heme, but absorption and resonance Raman spectroscopy indicate that the water coordinated to the iron atom is lost in several of the Gly-139 mutants, giving rise to mixtures of hexacoordinate and pentacoordinate ligation states. The active site perturbation is greatest when large amino acid side chains are introduced. Of the Gly-139 mutants investigated, only G139A catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, but most of them exhibit a new H2O2-dependent guaiacol peroxidation activity. The Gly-143 mutants, all of which have lost the water ligand, have no heme oxygenase or peroxidase activity. The results establish the importance of Gly-139 and Gly-143 in maintaining the appropriate environment for the heme oxygenase reaction and show that Gly-139 mutations disrupt this environment, probably by displacing the distal helix, converting heme oxygenase into a peroxidase. The principal role of the heme oxygenase active site may be to suppress the ferryl species formation responsible for peroxidase activity.
Nature Structural & Molecular Biology | 1997
Michael Gajhede; David J. Schuller; Anette Henriksen; Andrew T. Smith; Thomas L. Poulos
Nature Structural & Molecular Biology | 1995
David J. Schuller; Gregory A. Grant; Leonard J. Banaszak
Biochemistry | 2001
David J. Schuller; Wenming Zhu; Igor Stojiljkovic; and Angela Wilks; Thomas L. Poulos
Biochemistry | 2003
Jessica Rae O'brien; David J. Schuller; Victoria S. Yang; Bret D. Dillard; William N. Lanzilotta
Journal of Biological Chemistry | 2003
Latesh Lad; David J. Schuller; Hideaki Shimizu; Jonathan Friedman; Huiying Li; Paul R. Ortiz de Montellano; Thomas L. Poulos
Biochemistry | 2001
Hideaki Shimizu; David J. Schuller; William N. Lanzilotta; M. Sundaramoorthy; David M. Arciero; and Alan B. Hooper; Thomas L. Poulos