4n58
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4n58]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_brasiliense_PBR1692 Pectobacterium brasiliense PBR1692]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N58 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4n58]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_brasiliense_PBR1692 Pectobacterium brasiliense PBR1692]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N58 FirstGlance]. <br> | ||
| - | </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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=4n58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n58 OCA], [https://pdbe.org/4n58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n58 RCSB], [https://www.ebi.ac.uk/pdbsum/4n58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n58 ProSAT]</span></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=4n58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n58 OCA], [https://pdbe.org/4n58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n58 RCSB], [https://www.ebi.ac.uk/pdbsum/4n58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n58 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A067XG75_9GAMM A0A067XG75_9GAMM] | [https://www.uniprot.org/uniprot/A0A067XG75_9GAMM A0A067XG75_9GAMM] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The colicin-like bacteriocins are potent protein antibiotics that have evolved to efficiently cross the outer membrane of Gram-negative bacteria by parasitising nutrient uptake systems. We have structurally characterised the colicin M-like bacteriocin, pectocin M2, which is active against strains of Pectobacterium spp. This unusual bacteriocin lacks the intrinsically unstructured translocation domain that usually mediates translocation of these bacteriocins across the outer membrane, containing only a single globular ferredoxin domain connected to its cytotoxic domain by a flexible alpha-helix, which allows it to adopt two distinct conformations in solution. The ferredoxin domain of pectocin M2 is homologous to plant ferredoxins and allows pectocin M2 to parasitize a system utilised by Pectobacterium to obtain iron during infection of plants. Furthermore, we identify a novel ferredoxin-containing bacteriocin pectocin P, which possesses a cytotoxic domain homologous to lysozyme, illustrating that the ferredoxin domain acts as a generic delivery module for cytotoxic domains in Pectobacterium. | ||
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| - | Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake.,Grinter R, Josts I, Zeth K, Roszak AW, McCaughey LC, Cogdell RJ, Milner JJ, Kelly SM, Byron O, Walker D Mol Microbiol. 2014 May 28. doi: 10.1111/mmi.12655. PMID:24865810<ref>PMID:24865810</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4n58" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure of Pectocin M2 at 1.86 Angstroms
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