2ff7

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[[Image:2ff7.png|left|200px]]
 
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==The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state==
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The line below this paragraph, containing "STRUCTURE_2ff7", creates the "Structure Box" on the page.
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<StructureSection load='2ff7' size='340' side='right'caption='[[2ff7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ff7]] is a 1 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=2FF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FF7 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]] 1.6&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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{{STRUCTURE_2ff7| PDB=2ff7 | SCENE= }}
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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=2ff7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ff7 OCA], [https://pdbe.org/2ff7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ff7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ff7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ff7 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/ff/2ff7_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=2ff7 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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===The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ff7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16858415 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16858415}}
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==About this Structure==
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[[2ff7]] is a 1 chain structure of [[ABC transporter]] with 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=2FF7 OCA].
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==See Also==
==See Also==
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*[[ABC transporter]]
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:16858415</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Holland, I B.]]
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[[Category: Large Structures]]
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[[Category: Jenewein, S.]]
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[[Category: Holland IB]]
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[[Category: Jumpertz, T.]]
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[[Category: Jenewein S]]
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[[Category: Oswald, C.]]
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[[Category: Jumpertz T]]
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[[Category: Schmitt, L.]]
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[[Category: Oswald C]]
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[[Category: Zaitseva, J.]]
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[[Category: Schmitt L]]
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[[Category: Abc-transporter]]
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[[Category: Zaitseva J]]
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[[Category: Transport protein]]
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Current revision

The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state

PDB ID 2ff7

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