|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='3m7j' size='340' side='right'caption='[[3m7j]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='3m7j' size='340' side='right'caption='[[3m7j]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3m7j]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M7J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3m7j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M7J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</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]] 2.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m7h|3m7h]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene></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=3m7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7j OCA], [http://pdbe.org/3m7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m7j RCSB], [http://www.ebi.ac.uk/pdbsum/3m7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7j 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=3m7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7j OCA], [https://pdbe.org/3m7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m7j RCSB], [https://www.ebi.ac.uk/pdbsum/3m7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8GEJ9_PSEPU Q8GEJ9_PSEPU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garcia-Pino, A]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Loris, R]] | + | [[Category: Garcia-Pino A]] |
| - | [[Category: Antimicrobial protein]]
| + | [[Category: Loris R]] |
| - | [[Category: Bacterial toxin]]
| + | |
| - | [[Category: Bacteriocin]]
| + | |
| - | [[Category: Llpa]]
| + | |
| - | [[Category: Mannose]]
| + | |
| - | [[Category: Monocot mannose-binding lectin]]
| + | |
| - | [[Category: Protein-sugar complex]] | + | |
| - | [[Category: Pseudomona]]
| + | |
| - | [[Category: Sira]]
| + | |
| Structural highlights
Function
Q8GEJ9_PSEPU
Publication Abstract from PubMed
Lectin-like bacteriotoxic proteins, identified in several plant-associated bacteria, are able to selectively kill closely related species, including several phytopathogens, such as Pseudomonas syringae and Xanthomonas species, but so far their mode of action remains unrevealed. The crystal structure of LlpABW, the prototype lectin-like bacteriocin from Pseudomonas putida, reveals an architecture of two monocot mannose-binding lectin (MMBL) domains and a C-terminal beta-hairpin extension. The C-terminal MMBL domain (C-domain) adopts a fold very similar to MMBL domains from plant lectins and contains a binding site for mannose and oligomannosides. Mutational analysis indicates that an intact sugar-binding pocket in this domain is crucial for bactericidal activity. The N-terminal MMBL domain (N-domain) adopts the same fold but is structurally more divergent and lacks a functional mannose-binding site. Differential activity of engineered N/C-domain chimers derived from two LlpA homologues with different killing spectra, disclosed that the N-domain determines target specificity. Apparently this bacteriocin is assembled from two structurally similar domains that evolved separately towards dedicated functions in target recognition and bacteriotoxicity.
Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA.,Ghequire MG, Garcia-Pino A, Lebbe EK, Spaepen S, Loris R, De Mot R PLoS Pathog. 2013 Feb;9(2):e1003199. doi: 10.1371/journal.ppat.1003199. Epub 2013, Feb 28. PMID:23468636[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghequire MG, Garcia-Pino A, Lebbe EK, Spaepen S, Loris R, De Mot R. Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA. PLoS Pathog. 2013 Feb;9(2):e1003199. doi: 10.1371/journal.ppat.1003199. Epub 2013, Feb 28. PMID:23468636 doi:http://dx.doi.org/10.1371/journal.ppat.1003199
|
