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| <StructureSection load='6mpz' size='340' side='right'caption='[[6mpz]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6mpz' size='340' side='right'caption='[[6mpz]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6mpz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_c6a11 Lachnospiraceae bacterium c6a11] and [http://en.wikipedia.org/wiki/Promm Promm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MPZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MPZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mpz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_C6A11 Lachnospiraceae bacterium C6A11] and [https://en.wikipedia.org/wiki/Prochlorococcus_marinus_str._MIT_9313 Prochlorococcus marinus str. MIT 9313]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MPZ FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=16P:3,6,9,12,15,18-HEXAOXAICOSANE'>16P</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]] 2Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=16P:3,6,9,12,15,18-HEXAOXAICOSANE'>16P</scene>, <scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</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=6mpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mpz OCA], [http://pdbe.org/6mpz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mpz RCSB], [http://www.ebi.ac.uk/pdbsum/6mpz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mpz 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=6mpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mpz OCA], [https://pdbe.org/6mpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mpz RCSB], [https://www.ebi.ac.uk/pdbsum/6mpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mpz ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Lachnospiraceae bacterium c6a11]] | + | [[Category: Lachnospiraceae bacterium C6A11]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Promm]] | + | [[Category: Prochlorococcus marinus str. MIT 9313]] |
- | [[Category: Dong, S H]] | + | [[Category: Dong S-H]] |
- | [[Category: Nair, S K]] | + | [[Category: Nair SK]] |
- | [[Category: Lantibiotic]]
| + | |
- | [[Category: Leader peptide]]
| + | |
- | [[Category: Peptidase c39 domain]]
| + | |
- | [[Category: Peptide secretion]]
| + | |
- | [[Category: Transport protein]]
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| Structural highlights
Publication Abstract from PubMed
The secretion of peptides and proteins is essential for survival and ecological adaptation of bacteria. Dual-functional ATP-binding cassette transporters export antimicrobial or quorum signaling peptides in Gram-positive bacteria. Their substrates contain a leader sequence that is excised by an N-terminal peptidase C39 domain at a double Gly motif. We characterized the protease domain (LahT150) of a transporter from a lanthipeptide biosynthetic operon in Lachnospiraceae and demonstrate that this protease can remove the leader peptide from a diverse set of peptides. The 2.0 A resolution crystal structure of the protease domain in complex with a covalently bound leader peptide demonstrates the basis for substrate recognition across the entire class of such transporters. The structural data also provide a model for understanding the role of leader peptide recognition in the translocation cycle, and the function of degenerate, non-functional C39-like domains (CLD) in substrate recruitment in toxin exporters in Gram-negative bacteria.
Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease.,Bobeica SC, Dong SH, Huo L, Mazo N, McLaughlin MI, Jimenez-Oses G, Nair SK, van der Donk WA Elife. 2019 Jan 14;8. pii: 42305. doi: 10.7554/eLife.42305. PMID:30638446[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bobeica SC, Dong SH, Huo L, Mazo N, McLaughlin MI, Jimenez-Oses G, Nair SK, van der Donk WA. Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease. Elife. 2019 Jan 14;8. pii: 42305. doi: 10.7554/eLife.42305. PMID:30638446 doi:http://dx.doi.org/10.7554/eLife.42305
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