2hnb: Difference between revisions

Revision as of 14:12, 28 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:2hnb.png

Template:STRUCTURE 2hnb

Solution Structure of a bacterial holo-flavodoxinSolution Structure of a bacterial holo-flavodoxin

Template:ABSTRACT PUBMED 16963438

About this StructureAbout this Structure

2HNB is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: implications for cofactor binding and electron transfer., Hu Y, Li Y, Zhang X, Guo X, Xia B, Jin C, J Biol Chem. 2006 Nov 17;281(46):35454-66. Epub 2006 Sep 8. PMID:16963438

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 {{STRUCTURE_2hnb|  PDB=2hnb  |  SCENE=  }}
-'''Solution Structure of a bacterial holo-flavodoxin'''
+===Solution Structure of a bacterial holo-flavodoxin===
-==Overview==
+<!--
-Flavodoxins play central roles in the electron transfer involving various biological processes in microorganisms. The mioC gene of Escherichia coli encodes a 16-kDa flavodoxin and locates next to the chromosomal replication initiation origin (oriC). Extensive researches have been carried out to investigate the relationship between mioC transcription and replication initiation. Recently, the MioC protein was proposed to be essential for the biotin synthase activity in vitro. Nevertheless, the exact role of MioC in biotin synthesis and its physiological function in vivo remain elusive. In order to understand the molecular basis of the biological functions of MioC and the cofactor-binding mechanisms of flavodoxins, we have determined the solution structures of both the apo- and holo-forms of E. coli MioC protein at high resolution by nuclear magnetic resonance spectroscopy. The overall structures of both forms consist of an alpha/beta sandwich, which highly resembles the classical flavodoxin fold. However, significant diversities are observed between the two forms, especially the stabilization of the FMN-binding loops and the notable extension of secondary structures upon FMN binding. Structural comparison reveals fewer negative charged and aromatic residues near the FMN-binding site of MioC, as compared with that of flavodoxin 1 from E. coli, which may affect both the redox potentials and the redox partner interactions. Furthermore, the backbone dynamics studies reveal the conformational flexibility at different time scales for both apo- and holo-forms of MioC, which may play important roles for cofactor binding and electron transfer.
+The line below this paragraph, {{ABSTRACT_PUBMED_16963438}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16963438}}
 ==About this Structure==
-HNB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNB OCA].
+HNB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNB OCA].
 ==Reference==
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 [[Category: Alpha-beta sandwich]]
 [[Category: Flavodoxin fold]]
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