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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4kkq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_MJ-1236 Vibrio cholerae MJ-1236]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4kkq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_MJ-1236 Vibrio cholerae MJ-1236]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKQ FirstGlance]. <br>
</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=4kkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkq OCA], [https://pdbe.org/4kkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kkq RCSB], [https://www.ebi.ac.uk/pdbsum/4kkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkq ProSAT]</span></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]] 2.16&#8491;</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=4kkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkq OCA], [https://pdbe.org/4kkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kkq RCSB], [https://www.ebi.ac.uk/pdbsum/4kkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkq ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During the transition from a free-swimming, single-cell life-style to a sessile, multicellular state called a biofilm, bacteria produce and secrete an extracellular matrix comprised of nucleic acids, exopolysaccharides and adhesion proteins. The Vibrio cholerae biofilm matrix contains three major protein components, RbmA, Bap1 and RbmC, which are unique to Vibrio cholerae and appear to support biofilm formation at particular steps in the process. Here, we focus on RbmA, a structural protein with an unknown fold. RbmA participates in the early cell-cell adhesion events, and is found throughout the biofilm where it localizes to cell-cell contact sites. We determined crystal structures of RbmA and revealed that the protein folds into tandem fibronectin III (FnIII) folds. The protein is dimeric in solution and in crystals, with the dimer interface displaying a surface groove that is lined with several positively charged residues. Structure-guided mutagenesis studies establish a crucial role for this surface patch for RbmA function. Based on the structure, we hypothesize that RbmA serves as a tether by maintaining flexible linkages between cells and the extracellular matrix.
Structural basis for biofilm formation via the Vibrio cholerae matrix protein RbmA.,Giglio KM, Fong JC, Yildiz FH, Sondermann H J Bacteriol. 2013 May 17. PMID:23687270<ref>PMID:23687270</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kkq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 12:13, 1 March 2024

Crystal structure of Vibrio cholerae RbmA (crystal form 1)

4kkq, resolution 2.16Å

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