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4fzn

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==Crystal structure of syringacin M mutant D232A from Pseudomonas syringae pv. tomato DC3000==
==Crystal structure of syringacin M mutant D232A from Pseudomonas syringae pv. tomato DC3000==
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<StructureSection load='4fzn' size='340' side='right' caption='[[4fzn]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
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<StructureSection load='4fzn' size='340' side='right'caption='[[4fzn]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fzn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Psesm Psesm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FZN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato_str._DC3000 Pseudomonas syringae pv. tomato str. DC3000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FZN FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xmx|2xmx]], [[4fzl|4fzl]], [[4fzm|4fzm]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.12&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSPTO_0572 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223283 PSESM])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzn OCA], [https://pdbe.org/4fzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzn RCSB], [https://www.ebi.ac.uk/pdbsum/4fzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzn ProSAT]</span></td></tr>
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<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=4fzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzn OCA], [http://pdbe.org/4fzn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fzn RCSB], [http://www.ebi.ac.uk/pdbsum/4fzn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzn ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q88A25_PSESM Q88A25_PSESM]
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Colicin-like bacteriocins show potential as next generation antibiotics with clinical and agricultural applications. Key to these potential applications is their high potency and species specificity that enables a single pathogenic species to be targeted with minimal disturbance of the wider microbial community. Here we present the structure and function of the colicin M-like bacteriocin, syringacin M from Pseudomonas syringae pv. tomato DC3000. Syringacin M kills susceptible cells through a highly specific phosphatase activity that targets lipid II, ultimately inhibiting peptidoglycan synthesis. Comparison of the structures of syringacin M and colicin M reveal that in addition to the expected similarity between the homologous C-terminal catalytic domains, the receptor binding domains of these proteins, which share no discernible sequence homology, share a striking structural similarity. This indicates that the generation of the novel receptor binding and species specificities of these bacteriocins has been driven by diversifying selection rather than diversifying recombination as previously suggested. Additionally, the structure of syringacin M reveals the presence of an active site calcium ion that is coordinated by a conserved aspartic acid side chain and is essential for catalytic activity. We show that mutation of this residue to alanine inactivates syringacin M and that the metal ion is absent from the structure of the mutant protein. Consistent with the presence of Ca2+ in the active site, we show that syringacin M activity is supported by Ca2+, along with Mg2+ and Mn2+ and the protein is catalytically inactive in the absence of these ions.
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The crystal structure of the lipid II-degrading bacteriocin syringacin M suggests unexpected evolutionary relationships between colicin M-like bacteriocins.,Grinter R, Roszak AW, Cogdell RJ, Milner JJ, Walker D J Biol Chem. 2012 Sep 20. PMID:22995910<ref>PMID:22995910</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fzn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Psesm]]
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[[Category: Large Structures]]
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[[Category: Cogdell, J R]]
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[[Category: Pseudomonas syringae pv. tomato str. DC3000]]
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[[Category: Grinter, R]]
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[[Category: Cogdell JR]]
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[[Category: Roszak, A W]]
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[[Category: Grinter R]]
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[[Category: Walker, D]]
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[[Category: Roszak AW]]
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[[Category: Antimicrobial protein]]
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[[Category: Walker D]]
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[[Category: Phosphatase]]
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Current revision

Crystal structure of syringacin M mutant D232A from Pseudomonas syringae pv. tomato DC3000

PDB ID 4fzn

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