View source for 2alj


==Structure of the cis confomer of the major extracytoplasmic domain of the bacterial cell division protein divib from geobacillus stearothermophilus==
<StructureSection load='2alj' size='340' side='right'caption='[[2alj]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2alj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2alj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2alj OCA], [https://pdbe.org/2alj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2alj RCSB], [https://www.ebi.ac.uk/pdbsum/2alj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2alj ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/DIVIB_GEOKA DIVIB_GEOKA] Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.[HAMAP-Rule:MF_00912]
== 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/al/2alj_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/main_output.php?pdb_ID=2alj ConSurf].
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== Publication Abstract from PubMed ==
Bacterial cytokinesis requires the coordinated assembly of a complex of proteins, collectively known as the divisome, at the incipient division site. DivIB/FtsQ is a conserved component of the divisome in bacteria with cell walls, suggesting that it plays a role in synthesis and/or remodeling of septal peptidoglycan. We demonstrate that the extracytoplasmic region of DivIB comprises three discrete domains that we designate alpha, beta, and gamma from the N to C terminus. The alpha-domain is proximal to the cytoplasmic membrane and coincident with the polypeptide transport-associated domain that was proposed previously to function as a molecular chaperone. The beta-domain has a unique 3D fold, with no eukaryotic counterpart, and we show that it interconverts between two discrete conformations via cis-trans isomerization of a Tyr-Pro peptide bond. We propose that this isomerization might modulate protein-protein interactions of the flanking alpha- and gamma-domains. The C-terminal gamma-domain is unstructured in the absence of other divisomal proteins, but we show that it is critical for DivIB function.

Domain architecture and structure of the bacterial cell division protein DivIB.,Robson SA, King GF Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6700-5. Epub 2006 Apr 17. PMID:16618922<ref>PMID:16618922</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2alj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: King GF]]
[[Category: Robson SA]]