7ul6: Difference between revisions

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-'''Unreleased structure'''
-The entry 7ul6 is ON HOLD
+==CryoEM structure of full-length dimeric ClbP==
+<StructureSection load='7ul6' size='340' side='right'caption='[[7ul6]], [[Resolution|resolution]] 3.73&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7ul6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UL6 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.73&#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=7ul6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ul6 OCA], [https://pdbe.org/7ul6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ul6 RCSB], [https://www.ebi.ac.uk/pdbsum/7ul6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ul6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q0P7K6_ECOLX Q0P7K6_ECOLX]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Colibactin, a DNA cross-linking agent produced by gut bacteria, is implicated in colorectal cancer. Its biosynthesis uses a prodrug resistance mechanism: a non-toxic precursor assembled in the cytoplasm is activated after export to the periplasm. This activation is mediated by ClbP, an inner-membrane peptidase with an N-terminal periplasmic catalytic domain and a C-terminal three-helix transmembrane domain. Although the transmembrane domain is required for colibactin activation, its role in catalysis is unclear. Our structure of full-length ClbP bound to a product analog reveals an interdomain interface important for substrate binding and enzyme stability and interactions that explain the selectivity of ClbP for the N-acyl-D-asparagine prodrug motif. Based on structural and biochemical evidence, we propose that ClbP dimerizes to form an extended substrate-binding site that can accommodate a pseudodimeric precolibactin with its two terminal prodrug motifs in the two ClbP active sites, thus enabling the coordinated activation of both electrophilic warheads.
-Authors:
+Structural basis of colibactin activation by the ClbP peptidase.,Velilla JA, Volpe MR, Kenney GE, Walsh RM Jr, Balskus EP, Gaudet R Nat Chem Biol. 2023 Feb;19(2):151-158. doi: 10.1038/s41589-022-01142-z. Epub 2022 , Oct 17. PMID:36253550<ref>PMID:36253550</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7ul6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli CFT073]]
+[[Category: Large Structures]]
+[[Category: Gaudet R]]
+[[Category: Velilla JA]]
+[[Category: Walsh Jr RM]]