1J77

Crystal Structure of Gram-negative Bacterial Heme Oxygenase Complexed with Heme

Summary for 1J77

• Entry DOI: 10.2210/pdb1j77/pdb
• Related: 1DVE 1DVG 1QQ8
• Descriptor: HemO, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: proximal histidine, distal helix, oxidoreductase
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 1
• Total formula weight: 24226.10

Authors

Schuller, D.J.,Zhu, W.,Stojiljkovic, I.,Wilks, A.,Poulos, T.L. (deposition date: 2001-05-15, release date: 2001-05-30, Last modification date: 2024-02-07)

Primary citation

Schuller, D.J.,Zhu, W.,Stojiljkovic, I.,Wilks, A.,Poulos, T.L.
Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1.
Biochemistry, 40:11552-11558, 2001

PubMed Abstract: 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.

PubMed: 11560504
DOI: 10.1021/bi0110239

Experimental method

X-RAY DIFFRACTION (1.5 Å)