2ffa

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[[Image:2ffa.gif|left|200px]]<br /><applet load="2ffa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ffa.gif|left|200px]]
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caption="2ffa, resolution 1.70&Aring;" />
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'''Crystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADP'''<br />
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{{Structure
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|PDB= 2ffa |SIZE=350|CAPTION= <scene name='initialview01'>2ffa</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY=
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|GENE= hlyB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFA OCA].
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2FFA 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=2FFA OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16858415 16858415]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16858415 16858415]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: atpase]]
[[Category: atpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:51:41 2008''

Revision as of 14:51, 20 March 2008

Image:2ffa.gif


PDB ID 2ffa

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: and
Gene: hlyB (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

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

Reference

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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