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| - | [[Image:1dgg.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dgg.png|left|200px]] |
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| | {{STRUCTURE_1dgg| PDB=1dgg | SCENE= }} | | {{STRUCTURE_1dgg| PDB=1dgg | SCENE= }} |
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| - | '''HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX'''
| + | ===HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX=== |
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| - | ==Overview==
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| - | Human catalase is an heme-containing peroxisomal enzyme that breaks down hydrogen peroxide to water and oxygen; it is implicated in ethanol metabolism, inflammation, apoptosis, aging and cancer. The 1. 5 A resolution human enzyme structure, both with and without bound NADPH, establishes the conserved features of mammalian catalase fold and assembly, implicates Tyr370 as the tyrosine radical, suggests the structural basis for redox-sensitive binding of cognate mRNA via the catalase NADPH binding site, and identifies an unexpectedly substantial number of water-mediated domain contacts. A molecular ruler mechanism based on observed water positions in the 25 A-long channel resolves problems for selecting hydrogen peroxide. Control of water-mediated hydrogen bonds by this ruler selects for the longer hydrogen peroxide and explains the paradoxical effects of mutations that increase active site access but lower catalytic rate. The heme active site is tuned without compromising peroxide binding through a Tyr-Arg-His-Asp charge relay, arginine residue to heme carboxylate group hydrogen bonding, and aromatic stacking. Structures of the non-specific cyanide and specific 3-amino-1,2, 4-triazole inhibitor complexes of human catalase identify their modes of inhibition and help reveal the catalytic mechanism of catalase. Taken together, these resting state and inhibited human catalase structures support specific, structure-based mechanisms for the catalase substrate recognition, reaction and inhibition and provide a molecular basis for understanding ethanol intoxication and the likely effects of human polymorphisms.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10656833}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10656833 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10656833}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrogen peroxide]] | | [[Category: Hydrogen peroxide]] |
| | [[Category: Nadph]] | | [[Category: Nadph]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:49:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:02:47 2008'' |
Revision as of 20:02, 30 June 2008
Template:STRUCTURE 1dgg
HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX
Template:ABSTRACT PUBMED 10656833
About this Structure
1DGG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism., Putnam CD, Arvai AS, Bourne Y, Tainer JA, J Mol Biol. 2000 Feb 11;296(1):295-309. PMID:10656833
Page seeded by OCA on Mon Jun 30 23:02:47 2008
