7ry6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution NMR structural bundle of the first cyclization domain from yersiniabactin synthetase (Cy1) impacted by dynamics== | |
| + | <StructureSection load='7ry6' size='340' side='right'caption='[[7ry6]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7ry6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RY6 FirstGlance]. <br> | ||
| + | </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=7ry6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ry6 OCA], [https://pdbe.org/7ry6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ry6 RCSB], [https://www.ebi.ac.uk/pdbsum/7ry6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ry6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biological activity is governed by the timely redistribution of molecular interactions, and static structural snapshots often appear insufficient to provide the molecular determinants that choreograph communication. This conundrum applies to multidomain enzymatic systems called nonribosomal peptide synthetases (NRPSs), which assemble simple substrates into complex metabolites, where a dynamic domain organization challenges rational design to produce new pharmaceuticals. Using a nuclear magnetic resonance (NMR) atomic-level readout of biochemical transformations, we demonstrate that global structural fluctuations help promote substrate-dependent communication and allosteric responses, and impeding these global dynamics by a point-site mutation hampers allostery and molecular recognition. Our results establish global structural dynamics as sensors of molecular events that can remodel domain interactions, and they provide new perspectives on mechanisms of allostery, protein communication, and NRPS synthesis. | ||
| - | + | Global protein dynamics as communication sensors in peptide synthetase domains.,Mishra SH, Kancherla AK, Marincin KA, Bouvignies G, Nerli S, Sgourakis N, Dowling DP, Frueh DP Sci Adv. 2022 Jul 15;8(28):eabn6549. doi: 10.1126/sciadv.abn6549. Epub 2022 Jul, 15. PMID:35857508<ref>PMID:35857508</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7ry6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Yersinia pestis]] | ||
| + | [[Category: Bouvignies G]] | ||
| + | [[Category: Dowling DP]] | ||
| + | [[Category: Frueh DP]] | ||
| + | [[Category: Kancherla AK]] | ||
| + | [[Category: Marincin KA]] | ||
| + | [[Category: Mishra SH]] | ||
| + | [[Category: Nerli S]] | ||
| + | [[Category: Sgourakis NG]] | ||
Current revision
Solution NMR structural bundle of the first cyclization domain from yersiniabactin synthetase (Cy1) impacted by dynamics
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