7kw0: Difference between revisions
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7kw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kw0 OCA], [https://pdbe.org/7kw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kw0 RCSB], [https://www.ebi.ac.uk/pdbsum/7kw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kw0 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=7kw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kw0 OCA], [https://pdbe.org/7kw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kw0 RCSB], [https://www.ebi.ac.uk/pdbsum/7kw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kw0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains. | |||
Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.,Izore T, Candace Ho YT, Kaczmarski JA, Gavriilidou A, Chow KH, Steer DL, Goode RJA, Schittenhelm RB, Tailhades J, Tosin M, Challis GL, Krenske EH, Ziemert N, Jackson CJ, Cryle MJ Nat Commun. 2021 May 4;12(1):2511. doi: 10.1038/s41467-021-22623-0. PMID:33947858<ref>PMID:33947858</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7kw0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:25, 19 May 2021
Non-ribosomal didomain (stabilised glycine-PCP-C) acceptor bound stateNon-ribosomal didomain (stabilised glycine-PCP-C) acceptor bound state
Structural highlights
Publication Abstract from PubMedNon-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains. Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.,Izore T, Candace Ho YT, Kaczmarski JA, Gavriilidou A, Chow KH, Steer DL, Goode RJA, Schittenhelm RB, Tailhades J, Tosin M, Challis GL, Krenske EH, Ziemert N, Jackson CJ, Cryle MJ Nat Commun. 2021 May 4;12(1):2511. doi: 10.1038/s41467-021-22623-0. PMID:33947858[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||