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'''Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferrous state''' | '''Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferrous state''' | ||
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[[Category: Shiro, Y.]] | [[Category: Shiro, Y.]] | ||
[[Category: Unno, M.]] | [[Category: Unno, M.]] | ||
[[Category: | [[Category: Alpha helix]] | ||
[[Category: | [[Category: Bacterial iron acquisition]] | ||
[[Category: | [[Category: Riken structural genomics/proteomics initiative]] | ||
[[Category: | [[Category: Rsgi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:29:26 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:29, 2 May 2008
Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferrous state
OverviewOverview
Crystal structures of the ferric and ferrous heme complexes of HmuO, a 24-kDa heme oxygenase of Corynebacterium diphtheriae, have been refined to 1.4 and 1.5 A resolution, respectively. The HmuO structures show that the heme group is closely sandwiched between the proximal and distal helices. The imidazole group of His-20 is the proximal heme ligand, which closely eclipses the beta- and delta-meso axis of the porphyrin ring. A long range hydrogen bonding network is present, connecting the iron-bound water ligand to the solvent water molecule. This enables proton transfer from the solvent to the catalytic site, where the oxygen activation occurs. In comparison to the ferric complex, the proximal and distal helices move closer to the heme plane in the ferrous complex. Together with the kinked distal helix, this movement leaves only the alpha-meso carbon atom accessible to the iron-bound dioxygen. The heme pocket architecture is responsible for stabilization of the ferric hydroperoxo-active intermediate by preventing premature heterolytic O-O bond cleavage. This allows the enzyme to oxygenate selectively at the alpha-meso carbon in HmuO catalysis.
About this StructureAbout this Structure
1IW1 is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae., Hirotsu S, Chu GC, Unno M, Lee DS, Yoshida T, Park SY, Shiro Y, Ikeda-Saito M, J Biol Chem. 2004 Mar 19;279(12):11937-47. Epub 2003 Nov 26. PMID:14645223 Page seeded by OCA on Fri May 2 20:29:26 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Corynebacterium diphtheriae
- Heme oxygenase
- Single protein
- Chu, G C.
- Hirotsu, S.
- Ikeda-Saito, M.
- Lee, D S.
- Park, S Y.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Shiro, Y.
- Unno, M.
- Alpha helix
- Bacterial iron acquisition
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic