View source for 4cgk


==Crystal structure of the essential protein PcsB from Streptococcus pneumoniae==
<StructureSection load='4cgk' size='340' side='right'caption='[[4cgk]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cgk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_D39 Streptococcus pneumoniae D39]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CGK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=4cgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgk OCA], [https://pdbe.org/4cgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cgk RCSB], [https://www.ebi.ac.uk/pdbsum/4cgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2ZQ76_STRP2 A0A0H2ZQ76_STRP2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Separation of daughter cells during bacterial cell division requires splitting of the septal cross wall by peptidoglycan hydrolases. In Streptococcus pneumoniae, PcsB is predicted to perform this operation. Recent evidence shows that PcsB is recruited to the septum by the transmembrane FtsEX complex, and that this complex is required for cell division. However, PcsB lacks detectable catalytic activity in vitro, and while it has been proposed that FtsEX activates PcsB, evidence for this is lacking. Here we demonstrate that PcsB has muralytic activity, and report the crystal structure of full-length PcsB. The protein adopts a dimeric structure in which the V-shaped coiled-coil (CC) domain of each monomer acts as a pair of molecular tweezers locking the catalytic domain of each dimeric partner in an inactive configuration. This suggests that the release of the catalytic domains likely requires an ATP-driven conformational change in the FtsEX complex, conveyed towards the catalytic domains through coordinated movements of the CC domain.

Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae.,Bartual SG, Straume D, Stamsas GA, Munoz IG, Alfonso C, Martinez-Ripoll M, Havarstein LS, Hermoso JA Nat Commun. 2014 May 8;5:3842. doi: 10.1038/ncomms4842. PMID:24804636<ref>PMID:24804636</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cgk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae D39]]
[[Category: Alfonso C]]
[[Category: Bartual SG]]
[[Category: Havarstein LS]]
[[Category: Hermoso JA]]
[[Category: Martinez-Ripoll M]]
[[Category: Stamsas GA]]
[[Category: Straume D]]