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| | <StructureSection load='2fgk' size='340' side='right'caption='[[2fgk]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2fgk' size='340' side='right'caption='[[2fgk]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mt0|1mt0]], [[1xef|1xef]], [[2fgj|2fgj]], [[1ffa|1ffa]], [[1ffb|1ffb]]</div></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hlyB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| | <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> | | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Holland, I B]] | + | [[Category: Holland IB]] |
| - | [[Category: Jenewein, S]] | + | [[Category: Jenewein S]] |
| - | [[Category: Jumpertz, T]] | + | [[Category: Jumpertz T]] |
| - | [[Category: Oswald, C]] | + | [[Category: Oswald C]] |
| - | [[Category: Schmitt, L]] | + | [[Category: Schmitt L]] |
| - | [[Category: Zaitseva, J]] | + | [[Category: Zaitseva J]] |
| - | [[Category: Abc-cassette]]
| + | |
| - | [[Category: Abc-transporter]]
| + | |
| - | [[Category: Atp-loaded dimer]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zaitseva J, Oswald C, Jumpertz T, Jenewein S, Wiedenmann A, Holland IB, Schmitt L. A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 2006 Jul 26;25(14):3432-43. Epub 2006 Jul 6. PMID:16858415
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