5KZL

Structure of Heme Oxygenase from Leptospira interrogans

5KZL の概要

• エントリーDOI: 10.2210/pdb5kzl/pdb
• 分子名称: Heme oxygenase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: heme oxygenase leptospira, oxidoreductase
• 由来する生物種: Leptospira interrogans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24850.90

構造登録者

Klinke, S.,Soldano, A.,Otero, L.H.,Rivera, M.,Catalano-Dupuy, D.L.,Ceccarelli, E.A. (登録日: 2016-07-25, 公開日: 2017-07-26, 最終更新日: 2023-10-04)

主引用文献

Soldano, A.,Klinke, S.,Otero, L.H.,Rivera, M.,Catalano-Dupuy, D.L.,Ceccarelli, E.A.
Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.
PLoS ONE, 12:e0182535-e0182535, 2017

PubMed Abstract: Heme oxygenase from Leptospira interrogans is an important virulence factor. During catalysis, redox equivalents are provided to this enzyme by the plastidic-type ferredoxin-NADP+ reductase also found in L. interrogans. This process may have evolved to aid this bacterial pathogen to obtain heme-iron from their host and enable successful colonization. Herein we report the crystal structure of the heme oxygenase-heme complex at 1.73 Å resolution. The structure reveals several distinctive features related to its function. A hydrogen bonded network of structural water molecules that extends from the catalytic site to the protein surface was cleared observed. A depression on the surface appears to be the H+ network entrance from the aqueous environment to the catalytic site for O2 activation, a key step in the heme oxygenase reaction. We have performed a mutational analysis of the F157, located at the above-mentioned depression. The mutant enzymes were unable to carry out the complete degradation of heme to biliverdin since the reaction was arrested at the verdoheme stage. We also observed that the stability of the oxyferrous complex, the efficiency of heme hydroxylation and the subsequent conversion to verdoheme was adversely affected. These findings underscore a long-range communication between the outer fringes of the hydrogen-bonded network of structural waters and the heme active site during catalysis. Finally, by analyzing the crystal structures of ferredoxin-NADP+ reductase and heme oxygenase, we propose a model for the productive association of these proteins.

PubMed: 28771589
DOI: 10.1371/journal.pone.0182535

実験手法

X-RAY DIFFRACTION (1.73 Å)