1m6n: Difference between revisions

Revision as of 23:19, 2 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:1m6n.png

Template:STRUCTURE 1m6n

Crystal structure of the SecA translocation ATPase from Bacillus subtilisCrystal structure of the SecA translocation ATPase from Bacillus subtilis

Template:ABSTRACT PUBMED 12242434

About this StructureAbout this Structure

1M6N is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA., Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J, Science. 2002 Sep 20;297(5589):2018-26. PMID:12242434

Page seeded by OCA on Wed Jul 2 23:19:49 2008

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OCA

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-'''Crystal structure of the SecA translocation ATPase from Bacillus subtilis'''
+===Crystal structure of the SecA translocation ATPase from Bacillus subtilis===
-==Overview==
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-The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.
+The line below this paragraph, {{ABSTRACT_PUBMED_12242434}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12242434}}
 ==About this Structure==
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 [[Category: Protein translocation]]
 [[Category: Transmembrane transport]]
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