2fgk

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(New page: 200px<br /><applet load="2fgk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fgk, resolution 2.70&Aring;" /> '''Crystal structure of...)
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[[Image:2fgk.gif|left|200px]]<br /><applet load="2fgk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fgk, resolution 2.70&Aring;" />
 
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'''Crystal structure of the ABC-cassette E631Q mutant of HlyB with bound ATP'''<br />
 
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==Overview==
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==Crystal structure of the ABC-cassette E631Q mutant of HlyB with bound ATP==
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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.
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<StructureSection load='2fgk' size='340' side='right'caption='[[2fgk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FGK FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgk OCA], [https://pdbe.org/2fgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fgk RCSB], [https://www.ebi.ac.uk/pdbsum/2fgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fgk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HLYBP_ECOLX HLYBP_ECOLX] Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/2fgk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fgk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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:16858415<ref>PMID:16858415</ref>
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2FGK 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 ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FGK OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2fgk" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Holland, I.B.]]
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[[Category: Jenewein, S.]]
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[[Category: Jumpertz, T.]]
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[[Category: Oswald, C.]]
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[[Category: Schmitt, L.]]
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[[Category: Zaitseva, J.]]
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[[Category: ATP]]
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[[Category: abc-cassette]]
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[[Category: abc-transporter]]
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[[Category: atp-loaded dimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:32:40 2007''
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==See Also==
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Holland IB]]
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[[Category: Jenewein S]]
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[[Category: Jumpertz T]]
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[[Category: Oswald C]]
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[[Category: Schmitt L]]
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[[Category: Zaitseva J]]

Current revision

Crystal structure of the ABC-cassette E631Q mutant of HlyB with bound ATP

PDB ID 2fgk

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