View source for 6mpz


==Crystal structure of a double glycine motif protease from AMS/PCAT transporter in complex with the leader peptide==
<StructureSection load='6mpz' size='340' side='right'caption='[[6mpz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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'>[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>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:30638446</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mpz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lachnospiraceae bacterium C6A11]]
[[Category: Large Structures]]
[[Category: Prochlorococcus marinus str. MIT 9313]]
[[Category: Dong S-H]]
[[Category: Nair SK]]