3hjt
From Proteopedia
(Difference between revisions)
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- | + | ==Structure of laminin binding protein (Lmb) of Streptococcus agalactiae A bifunctional protein with adhesin and metal transporting activity== | |
- | + | <StructureSection load='3hjt' size='340' side='right' caption='[[3hjt]], [[Resolution|resolution]] 2.50Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3hjt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptoccocus_de_la_mammite"_nocard_and_mollereau_1887 "streptoccocus de la mammite" nocard and mollereau 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HJT FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1311 "Streptoccocus de la mammite" Nocard and Mollereau 1887])</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=3hjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hjt RCSB], [http://www.ebi.ac.uk/pdbsum/3hjt PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/3hjt_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Adhesion/invasion of pathogenic bacteria is a critical step in infection and is mediated by surface-exposed proteins termed adhesins. The crystal structure of recombinant Lmb, a laminin-binding adhesin from Streptococcus agalactiae, has been determined at 2.5 A resolution. Based on sequence and structural homology, Lmb was placed into the cluster 9 family of the ABC (ATP-binding cassette) transport system. The structural organization of Lmb closely resembles that of ABC-type solute-binding proteins (SBPs), in which two structurally related globular domains interact with each other to form a metal-binding cavity at the interface. The bound zinc in Lmb is tetrahedrally coordinated by three histidines and a glutamate from both domains. A comparison of Lmb with other metal transporters revealed an interesting feature of the dimerization of molecules in the crystallographic asymmetric unit in all zinc-binding transporters. A closer comparison of Lmb with the zinc-binding ZnuA from Escherichia coli and Synechocystis 6803 suggested that Lmb might undergo a unique structural rearrangement upon metal binding and release. The crystal structure of Lmb provides an impetus for further investigations into the molecular basis of laminin binding by human pathogens. Being ubiquitous in all serotypes of group B streptococcus (GBS), the structure of Lmb may direct the development of an efficient vaccine. | ||
- | + | Structure of laminin-binding adhesin (Lmb) from Streptococcus agalactiae.,Ragunathan P, Spellerberg B, Ponnuraj K Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1262-9. doi:, 10.1107/S0907444909038359. Epub 2009 Nov 17. PMID:19966412<ref>PMID:19966412</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Streptoccocus de la mammite nocard and mollereau 1887]] | [[Category: Streptoccocus de la mammite nocard and mollereau 1887]] | ||
- | [[Category: Ponnuraj, K | + | [[Category: Ponnuraj, K]] |
- | [[Category: Ragunathan, P | + | [[Category: Ragunathan, P]] |
- | [[Category: Spellerberg, B | + | [[Category: Spellerberg, B]] |
[[Category: Adhesin]] | [[Category: Adhesin]] | ||
[[Category: Atp binding cassette]] | [[Category: Atp binding cassette]] |
Revision as of 09:33, 20 January 2015
Structure of laminin binding protein (Lmb) of Streptococcus agalactiae A bifunctional protein with adhesin and metal transporting activity
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