4gdn

<StructureSection load='4gdn' size='340' side='right' caption='[[4gdn]], [[Resolution|resolution]] 3.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[4gdn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_n315 Staphylococcus aureus subsp. aureus n315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GDN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o3v|3o3v]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flp, SA2230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158879 Staphylococcus aureus subsp. aureus N315])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gdn RCSB], [http://www.ebi.ac.uk/pdbsum/4gdn PDBsum]</span></td></tr>

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== Publication Abstract from PubMed ==

pks genomic island of Escherichia coli is involved in the synthesis of the non-ribosomal peptide-type genotoxin colibactin, which has been suggesting as affecting the host immune response and having an impact on cancer development. The pks-encoded enzyme ClbP is an atypical peptidase that contributes to the synthesis of colibactin. In this work, we identified key features of ClbP. Bacterial fractionation and Western-blot analysis revealed the docking of ClbP to the bacterial inner membrane via a C-terminal domain harboring three predicted transmembrane helices. Whereas only one helix was necessary for the location in the inner membrane, the complete sequence of the C-terminal domain was necessary for ClbP bioactivity. In addition, the N-terminal sequence of ClbP allowed the SRP/Sec/YidC- and MreB-dependent translocation of the enzymatic domain in the periplasmic compartment, a feature also essential for ClbP bioactivity. Finally, the comparison of ClbP structure with that of the paralogs FmtA-like and AmpC revealed at an extremity of the catalytic groove a negative electrostatic potential surface characteristic of ClbP. Site-directed mutagenesis experiments identified in this zone two aspartic residues that were important for ClbP bioactivity. Overall, these results suggest a model for precolibactin activation by ClbP and pave a way for the design of inhibitors targeting colibactin production.

 

Analysis of Structure-Function Relationships in the Colibactin-Maturating Enzyme ClbP.,Cougnoux A, Gibold L, Robin F, Dubois D, Pradel N, Darfeuille-Michaud A, Dalmasso G, Delmas J, Bonnet R J Mol Biol. 2012 Oct 2. pii: S0022-2836(12)00782-6. doi:, 10.1016/j.jmb.2012.09.017. PMID:23041299<ref>PMID:23041299</ref>

 

[[Category: Staphylococcus aureus subsp. aureus n315]]

[[Category: Bonnet, R]]

[[Category: Cougnoux, A]]

[[Category: Dalmasso, G]]

[[Category: Delmas, J]]

[[Category: Gibold, L]]

[[Category: Robin, F]]

[[Category: Peptidase]]