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2q32

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[[Image:2q32.jpg|left|200px]]
 
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{{STRUCTURE_2q32| PDB=2q32 | SCENE= }}
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'''Crystal structure of human heme oxygenase-2 C127A (HO-2)'''
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===Crystal structure of human heme oxygenase-2 C127A (HO-2)===
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==Overview==
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Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.
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(as it appears on PubMed at http://www.pubmed.gov), where 17965015 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17965015}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:14:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:43:25 2008''

Revision as of 15:43, 28 July 2008

Template:STRUCTURE 2q32

Crystal structure of human heme oxygenase-2 C127A (HO-2)

Template:ABSTRACT PUBMED 17965015

About this Structure

2Q32 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:17965015

Page seeded by OCA on Mon Jul 28 18:43:25 2008

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