8jc1
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of Pectocin M1 from Pectobacterium carotovorum== | |
+ | <StructureSection load='8jc1' size='340' side='right'caption='[[8jc1]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[8jc1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JC1 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]] 2.04Å</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=8jc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jc1 OCA], [https://pdbe.org/8jc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jc1 RCSB], [https://www.ebi.ac.uk/pdbsum/8jc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jc1 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/C6DJ69_PECCP C6DJ69_PECCP] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Pectocin M1 (PM1), the bacteriocin from phytopathogenic Pectobacterium carotovorum which causes soft rot disease, has a unique ferredoxin domain that allows it to use FusA of the plant ferredoxin uptake system. To probe the structure-based mechanism of PM1 uptake, we determined the X-ray structure of full-length PM1, containing an N-terminal ferredoxin and C-terminal catalytic domain connected by helical linker, at 2.04 A resolution. Based on published FusA structure and NMR data for PM1 ferredoxin domain titrated with FusA, we modeled docking of the ferredoxin domain with FusA. Combining the docking models with the X-ray structures of PM1 and FusA enables us to propose the mechanism by which PM1 undergoes dynamic domain rearrangement to translocate across the target cell outer membrane. | ||
- | + | Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.,Jantarit N, Tanaka H, Lin Y, Lee YH, Kurisu G FEBS Open Bio. 2024 Aug 9. doi: 10.1002/2211-5463.13874. PMID:39123319<ref>PMID:39123319</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 8jc1" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: Kurisu | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Pectobacterium carotovorum]] | ||
+ | [[Category: Jantarit N]] | ||
+ | [[Category: Kurisu G]] | ||
+ | [[Category: Tanaka H]] |
Current revision
Crystal structure of Pectocin M1 from Pectobacterium carotovorum
|