1j77
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Crystal Structure of Gram-negative Bacterial Heme Oxygenase Complexed with Heme
OverviewOverview
We report the crystal structure of heme oxygenase from the pathogenic, bacterium Neisseria meningitidis at 1.5 A and compare and contrast it with, known structures of heme oxygenase-1 from mammalian sources. Both the, bacterial and mammalian enzymes share the same overall fold, with a, histidine contributing a ligand to the proximal side of the heme iron and, a kinked alpha-helix defining the distal pocket. The distal helix differs, noticeably in both sequence and conformation, and the distal pocket of the, Neisseria enzyme is substantially smaller than in the mammalian enzyme., Key glycine residues provide the flexibility for the helical kink, allow, close contact of the helix backbone with the heme, and may interact, directly with heme ligands.
About this StructureAbout this Structure
1J77 is a Single protein structure of sequence from Neisseria meningitidis with HEM as ligand. Active as Heme oxygenase, with EC number 1.14.99.3 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1., Schuller DJ, Zhu W, Stojiljkovic I, Wilks A, Poulos TL, Biochemistry. 2001 Sep 25;40(38):11552-8. PMID:11560504
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