View source for 2xxp


==A widespread family of bacterial cell wall assembly proteins==
<StructureSection load='2xxp' size='340' side='right'caption='[[2xxp]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xxp]] is a 1 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=2XXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XXP 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]] 1.692&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSL:MONO-TRANS,+OCTA-CIS+DECAPRENYL-PHOSPHATE'>DSL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=2xxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxp OCA], [https://pdbe.org/2xxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xxp RCSB], [https://www.ebi.ac.uk/pdbsum/2xxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9ZII9_STRP2 Q9ZII9_STRP2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Teichoic acids and acidic capsular polysaccharides are major anionic cell wall polymers (APs) in many bacteria, with various critical cell functions, including maintenance of cell shape and structural integrity, charge and cation homeostasis, and multiple aspects of pathogenesis. We have identified the widespread LytR-Cps2A-Psr (LCP) protein family, of previously unknown function, as novel enzymes required for AP synthesis. Structural and biochemical analysis of several LCP proteins suggest that they carry out the final step of transferring APs from their lipid-linked precursor to cell wall peptidoglycan (PG). In Bacillus subtilis, LCP proteins are found in association with the MreB cytoskeleton, suggesting that MreB proteins coordinate the insertion of the major polymers, PG and AP, into the cell wall.

A widespread family of bacterial cell wall assembly proteins.,Kawai Y, Marles-Wright J, Cleverley RM, Emmins R, Ishikawa S, Kuwano M, Heinz N, Bui NK, Hoyland CN, Ogasawara N, Lewis RJ, Vollmer W, Daniel RA, Errington J EMBO J. 2011 Sep 30. doi: 10.1038/emboj.2011.358. PMID:21964069<ref>PMID:21964069</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xxp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae D39]]
[[Category: Bui NK]]
[[Category: Cleverley RM]]
[[Category: Daniel RA]]
[[Category: Emmins R]]
[[Category: Errington J]]
[[Category: Heinz N]]
[[Category: Ishikawa S]]
[[Category: Kawai Y]]
[[Category: Kuwano M]]
[[Category: Lewis RJ]]
[[Category: Marles-Wright J]]
[[Category: Ogasawara N]]
[[Category: Vollmer W]]