2an0: Difference between revisions

Revision as of 03:07, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2an0.png

Template:STRUCTURE 2an0

Crystal Structure of the P332G mutant of the Bacillus subtilis NOSCrystal Structure of the P332G mutant of the Bacillus subtilis NOS

Template:ABSTRACT PUBMED 16126221

About this StructureAbout this Structure

2AN0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a loose dimer: an intermediate in nitric oxide synthase assembly., Pant K, Crane BR, J Mol Biol. 2005 Sep 30;352(4):932-40. PMID:16126221

Page seeded by OCA on Tue Jul 29 03:07:39 2008

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OCA

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-'''Crystal Structure of the P332G mutant of the Bacillus subtilis NOS'''
+===Crystal Structure of the P332G mutant of the Bacillus subtilis NOS===
-==Overview==
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-Cooperativity among ligand binding, subunit association, and protein folding has implications for enzyme regulation as well as protein aggregation events associated with disease. The binding of substrate l-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthases (NOSs) from a "loose dimer", with an exposed active center and higher sensitivity to proteolysis, to a "tight dimer" competent for catalysis. The crystallographic structure of the Bacillus subtilis NOS loose dimer shows an altered association state with severely destabilized subdomains. Ligand binding or heme reduction converts loose dimers to tight dimers in solution and crystals. Mutations at key positions in the dimer interface that distinguish prokaryotic from eukaryotic NOSs affect the propensity to form loose dimers. The loose dimer structure indicates that non-native interactions can mediate subunit association in NOS.
+The line below this paragraph, {{ABSTRACT_PUBMED_16126221}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16126221 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16126221}}
 ==About this Structure==
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 [[Category: P332g mutant]]
 [[Category: Prokaryotic nitric oxide synthase]]
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