1et5: Difference between revisions

Revision as of 01:55, 1 July 2008

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File:1et5.png

Template:STRUCTURE 1et5

CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6

Template:ABSTRACT PUBMED 10811642

About this StructureAbout this Structure

1ET5 is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.

ReferenceReference

Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase., Boulanger MJ, Kukimoto M, Nishiyama M, Horinouchi S, Murphy ME, J Biol Chem. 2000 Aug 4;275(31):23957-64. PMID:10811642

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OCA

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-'''CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6'''
+===CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6===
-==Overview==
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-Two active site residues, Asp-98 and His-255, of copper-containing nitrite reductase (NIR) from Alcaligenes faecalis have been mutated to probe the catalytic mechanism. Three mutations at these two sites (D98N, H255D, and H255N) result in large reductions in activity relative to native NIR, suggesting that both residues are involved intimately in the reaction mechanism. Crystal structures of these mutants have been determined using data collected to better than 1. 9-A resolution. In the native structure, His-255 Nepsilon2 forms a hydrogen bond through a bridging water molecule to the side chain of Asp-98, which also forms a hydrogen bond to a water or nitrite oxygen ligated to the active site copper. In the D98N mutant, reorientation of the Asn-98 side chain results in the loss of the hydrogen bond to the copper ligand water, consistent with a negatively charged Asp-98 directing the binding and protonation of nitrite in the native enzyme. An additional solvent molecule is situated between residues 255 and the bridging water in the H255N and H255D mutants and likely inhibits nitrite binding. The interaction of His-255 with the bridging water appears to be necessary for catalysis and may donate a proton to reaction intermediates in addition to Asp-98.
+The line below this paragraph, {{ABSTRACT_PUBMED_10811642}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10811642 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10811642}}
 ==About this Structure==
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 [[Category: Nishiyama, M.]]
 [[Category: Greek key beta barrel domain]]
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