2bmv
From Proteopedia
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Revision as of 14:38, 30 October 2007
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APOFLAVODOXIN FROM HELICOBACTER PYLORI
Overview
Flavodoxins, noncovalent complexes between apoflavodoxins and flavin, mononucleotide (FMN), are useful models to investigate the mechanism of, protein/flavin recognition. In this respect, the only available crystal, structure of an apoflavodoxin (that from Anabaena) showed a closed, isoalloxazine pocket and the presence of a bound phosphate ion, which, posed many questions on the recognition mechanism and on the potential, physiological role exerted by phosphate ions. To address these issues we, report here the X-ray structure of the apoflavodoxin from the pathogen, Helicobacter pylori. The protein naturally lacks one of the conserved, aromatic residues that close the isoalloxazine pocket in Anabaena, and the, structure has been determined in a medium lacking phosphate. In spite of, these ... [(full description)]
About this Structure
2BMV is a [Single protein] structure of sequence from [Helicobacter pylori] with CL and BEN as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Common conformational changes in flavodoxins induced by FMN and anion binding: The structure of Helicobacter pylori apoflavodoxin., Martinez-Julvez M, Cremades N, Bueno M, Perez-Dorado I, Maya C, Cuesta-Lopez S, Prada D, Falo F, Hermoso JA, Sancho J, Proteins. 2007 Jul 10;. PMID:17623845
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