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4bjp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of E. coli penicillin binding protein 3== | |
| + | <StructureSection load='4bjp' size='340' side='right'caption='[[4bjp]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bjp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BJP 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]] 2.5Å</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=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4bjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bjp OCA], [https://pdbe.org/4bjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bjp RCSB], [https://www.ebi.ac.uk/pdbsum/4bjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bjp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall peptidoglycan during cell division. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. We have solved the crystal structure of a soluble form of PBP3 (PBP357-577) at 2.5 A revealing the two modules of high molecular weight class B PBPs, a carboxy terminal module exhibiting transpeptidase activity and an amino terminal module of unknown function. To gain additional insight, the PBP3 Val88-Ser165 subdomain (PBP388-165), for which the electron density is poorly defined in the PBP3 crystal, was produced and its structure solved by SAD phasing at 2.1 A. The structure shows a three dimensional domain swapping with a beta-strand of one molecule inserted between two strands of the paired molecule, suggesting a possible role in PBP357-577 dimerization. | ||
| - | + | Crystal Structure of Penicillin-Binding Protein 3 (PBP3) from Escherichia coli.,Sauvage E, Derouaux A, Fraipont C, Joris M, Herman R, Rocaboy M, Schloesser M, Dumas J, Kerff F, Nguyen-Disteche M, Charlier P PLoS One. 2014 May 29;9(5):e98042. doi: 10.1371/journal.pone.0098042. eCollection, 2014. PMID:24875494<ref>PMID:24875494</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4bjp" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Charlier P]] | ||
| + | [[Category: Herman R]] | ||
| + | [[Category: Joris M]] | ||
| + | [[Category: Kerff F]] | ||
| + | [[Category: Rocaboy M]] | ||
| + | [[Category: Sauvage E]] | ||
Current revision
Crystal structure of E. coli penicillin binding protein 3
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Categories: Escherichia coli | Large Structures | Charlier P | Herman R | Joris M | Kerff F | Rocaboy M | Sauvage E
