2afi: Difference between revisions

Revision as of 13:01, 27 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:2afi.png

Template:STRUCTURE 2afi

Crystal Structure of MgADP bound Av2-Av1 ComplexCrystal Structure of MgADP bound Av2-Av1 Complex

Template:ABSTRACT PUBMED 16123301

About this StructureAbout this Structure

2AFI is a Protein complex structure of sequences from Azotobacter vinelandii. Full crystallographic information is available from OCA.

ReferenceReference

Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:16123301

Page seeded by OCA on Sun Jul 27 13:01:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of MgADP bound Av2-Av1 Complex'''
+===Crystal Structure of MgADP bound Av2-Av1 Complex===
-==Overview==
+<!--
-Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.
+The line below this paragraph, {{ABSTRACT_PUBMED_16123301}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16123301}}
 ==About this Structure==
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 [[Category: Nitrogen fixation]]
 [[Category: Oxidoreductase]]
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