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| | ==Structure of Bug27 from Bordetella pertussis== | | ==Structure of Bug27 from Bordetella pertussis== |
| - | <StructureSection load='2qpq' size='340' side='right' caption='[[2qpq]], [[Resolution|resolution]] 1.92Å' scene=''> | + | <StructureSection load='2qpq' size='340' side='right'caption='[[2qpq]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qpq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_tussis-convulsivae"_lehmann_and_neumann_1927 "bacterium tussis-convulsivae" lehmann and neumann 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QPQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qpq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QPQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 1.92Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f5x|2f5x]], [[2dvz|2dvz]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">2667749 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=520 "Bacterium tussis-convulsivae" Lehmann and Neumann 1927])</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=2qpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpq OCA], [https://pdbe.org/2qpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qpq RCSB], [https://www.ebi.ac.uk/pdbsum/2qpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qpq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpq OCA], [http://pdbe.org/2qpq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qpq RCSB], [http://www.ebi.ac.uk/pdbsum/2qpq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qpq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7W019_BORPE Q7W019_BORPE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qp/2qpq_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qp/2qpq_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium tussis-convulsivae lehmann and neumann 1927]] | + | [[Category: Bordetella pertussis]] |
| - | [[Category: Bompard, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Herrou, J]] | + | [[Category: Bompard C]] |
| - | [[Category: Alpha/beta domain]] | + | [[Category: Herrou J]] |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Venus flytrap]]
| + | |
| Structural highlights
Function
Q7W019_BORPE
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
Bug proteins form a large family of periplasmic solute-binding proteins well represented in beta-proteobacteria. They adopt a characteristic Venus flytrap fold with two globular domains bisected by a ligand-binding cleft. The structures of two liganded Bug proteins have revealed that the family is specific for carboxylated solutes, with a characteristic mode of binding involving two highly conserved beta strand-beta turn-alpha helix motifs originating from each domain. These two motifs form hydrogen bonds with a carboxylate group of the ligand, both directly and via conserved water molecules, and have thus been termed the carboxylate pincers. In both crystallized Bug proteins, the ligands were found enclosed between the two domains and inaccessible to solvent, suggesting an inter-domain hinge-bending motion upon ligand binding. We report here the first structures of an open, unliganded Bug protein and of the same protein with a citrate ion bound in the open cavity. One of the ligand carboxylate groups is bound to one half of the carboxylate pincers by the beta strand-beta turn-alpha helix motif from domain 1, and the citrate ion forms several additional interactions with domain 1. The ligand is accessible to solvent and has very few contacts with domain 2. In this open, liganded structure, the second part of the carboxylate pincers originating from domain 2 is not stabilized by ligand binding, and a loop replaces the beta turn. In the unliganded structure, both motifs of the carboxylate pincers are highly mobile, and neither of the two beta turns is formed. Thus, ligand recognition is performed by domain 1, with the carboxylate group serving as an initial anchoring point. Stabilization of the closed conformation requires proper interactions to be established with domain 2, and thus domain 2 discriminates between productively and non-productively bound ligands.
Structure-based mechanism of ligand binding for periplasmic solute-binding protein of the Bug family.,Herrou J, Bompard C, Antoine R, Leroy A, Rucktooa P, Hot D, Huvent I, Locht C, Villeret V, Jacob-Dubuisson F J Mol Biol. 2007 Nov 2;373(4):954-64. Epub 2007 Aug 19. PMID:17870093[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Herrou J, Bompard C, Antoine R, Leroy A, Rucktooa P, Hot D, Huvent I, Locht C, Villeret V, Jacob-Dubuisson F. Structure-based mechanism of ligand binding for periplasmic solute-binding protein of the Bug family. J Mol Biol. 2007 Nov 2;373(4):954-64. Epub 2007 Aug 19. PMID:17870093 doi:10.1016/j.jmb.2007.08.006
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