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1xk1

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{{STRUCTURE_1xk1| PDB=1xk1 | SCENE= }}
{{STRUCTURE_1xk1| PDB=1xk1 | SCENE= }}
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'''Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1'''
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===Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1===
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==Overview==
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Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Earlier mutagenesis work on human HO-1 showed that replacement of either Gly139 or Gly143 suppresses heme oxygenase activity and, in the case of the Gly139 mutants, increases peroxidase activity (Liu et al. in J. Biol. Chem. 275:34501, 2000). To further investigate the role of the conserved distal helix glycines, we have determined the crystal structures of the human HO-1 G139A mutant, the G139A mutant in a complex with NO, and the G143H mutant at 1.88, 2.18 and 2.08 A, respectively. The results confirm that fine tuning of the previously noted active-site hydrogen-bonding network is critical in determining whether heme oxygenase or peroxidase activity is observed.
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(as it appears on PubMed at http://www.pubmed.gov), where 15690204 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15690204}}
==About this Structure==
==About this Structure==
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[[Category: Heme]]
[[Category: Heme]]
[[Category: Heme degredation]]
[[Category: Heme degredation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:07:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:06:25 2008''

Revision as of 11:06, 29 July 2008

Image:1xk1.png

Template:STRUCTURE 1xk1

Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1

Template:ABSTRACT PUBMED 15690204

About this Structure

1XK1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity., Lad L, Koshkin A, de Montellano PR, Poulos TL, J Biol Inorg Chem. 2005 Mar;10(2):138-46. Epub 2005 Feb 3. PMID:15690204

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