2ffa: Difference between revisions

Revision as of 10:30, 29 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:2ffa.png

Template:STRUCTURE 2ffa

Crystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADPCrystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADP

Template:ABSTRACT PUBMED 16858415

About this StructureAbout this Structure

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

ReferenceReference

A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer., Zaitseva J, Oswald C, Jumpertz T, Jenewein S, Wiedenmann A, Holland IB, Schmitt L, EMBO J. 2006 Jul 26;25(14):3432-43. Epub 2006 Jul 6. PMID:16858415

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OCA

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 {{STRUCTURE_2ffa|  PDB=2ffa  |  SCENE=  }}
-'''Crystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADP'''
+===Crystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADP===
-==Overview==
+<!--
-The ATP-binding cassette (ABC)-transporter haemolysin (Hly)B, a central element of a Type I secretion machinery, acts in concert with two additional proteins in Escherichia coli to translocate the toxin HlyA directly from the cytoplasm to the exterior. The basic set of crystal structures necessary to describe the catalytic cycle of the isolated HlyB-NBD (nucleotide-binding domain) has now been completed. This allowed a detailed analysis with respect to hinge regions, functionally important key residues and potential energy storage devices that revealed many novel features. These include a structural asymmetry within the ATP dimer that was significantly enhanced in the presence of Mg2+, indicating a possible functional asymmetry in the form of one open and one closed phosphate exit tunnel. Guided by the structural analysis, we identified two amino acids, closing one tunnel by an apparent salt bridge. Mutation of these residues abolished ATP-dependent cooperativity of the NBDs. The implications of these new findings for the coupling of ATP binding and hydrolysis to functional activity are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16858415}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16858415 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16858415}}
 ==About this Structure==
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 [[Category: Abc-transporter]]
 [[Category: Atpase]]
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