2bmv
From Proteopedia
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| - | [[Image:2bmv.gif|left|200px]]<br /> | + | [[Image:2bmv.gif|left|200px]]<br /><applet load="2bmv" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bmv" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2bmv, resolution 2.11Å" /> | caption="2bmv, resolution 2.11Å" /> | ||
'''APOFLAVODOXIN FROM HELICOBACTER PYLORI'''<br /> | '''APOFLAVODOXIN FROM HELICOBACTER PYLORI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with CL and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2BMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with CL and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BMV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:52:48 2007'' |
Revision as of 16:43, 18 December 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 significant differences, the isoallozaxine pocket in H. pylori, apoflavodoxin appears also closed and a chloride ion is bound at a, native-like FMN phosphate site. It seems thus that it is a general, characteristic of apoflavodoxins to display closed, non-native, isoalloxazine binding sites together with native-like, rather promiscuous, phosphate binding sites that can bear other available small anions present, in solution. In this respect, both binding energy hot spots of the, apoflavodoxin/FMN complex are initially unavailable to FMN binding and the, specific spot for FMN recognition may depend on the dynamics of the two, candidate regions. Molecular dynamics simulations show that the, isoalloxazine binding loops are intrinsically flexible at physiological, temperatures, thus facilitating the intercalation of the cofactor, and, that their mobility is modulated by the anion bound at the phosphate site., Proteins 2007. (c) 2007 Wiley-Liss, Inc.
About this Structure
2BMV is a Single protein structure of sequence from Helicobacter pylori with CL and BEN as ligands. Known structural/functional Site: . 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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