1atg: Difference between revisions

Revision as of 17:33, 30 June 2008

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File:1atg.png

Template:STRUCTURE 1atg

AZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEINAZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEIN

Template:ABSTRACT PUBMED 9862806

About this StructureAbout this Structure

1ATG is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.

ReferenceReference

Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA., Lawson DM, Williams CE, Mitchenall LA, Pau RN, Structure. 1998 Dec 15;6(12):1529-39. PMID:9862806

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 {{STRUCTURE_1atg|  PDB=1atg  |  SCENE=  }}
-'''AZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEIN'''
+===AZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEIN===
-==Overview==
+<!--
-Background:. Periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. Nevertheless, almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. The ligand is bound at the bottom of a deep cleft, which lies at the interface between these two domains. The oxyanion-binding proteins are notable in that they can discriminate between very similar ligands. Results:. Azotobacter vinelandii is unusual in that it possesses two periplasmic molybdate-binding proteins. The crystal structure of one of these with bound ligand has been determined at 1.2 A resolution. It superficially resembles the structure of sulphate-binding protein (SBP) from Salmonella typhimurium and uses a similar constellation of hydrogen-bonding interactions to bind its ligand. However, the detailed interactions are distinct from those of SBP and the more closely related molybdate-binding protein of Escherichia coli. Conclusions:. Despite differences in the residues involved in binding, the volumes of the binding pockets in the A. vinelandii and E. coli molybdate-binding proteins are similar and are significantly larger than that of SBP. We conclude that the discrimination between molybdate and sulphate shown by these binding proteins is largely dependent upon small differences in the sizes of these two oxyanions.
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+{{ABSTRACT_PUBMED_9862806}}
 ==About this Structure==
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 [[Category: Periplasm]]
 [[Category: Tungstate]]
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