2n6y: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 2n6y is ON HOLD
+==Solution structure of holo ArCP from yersiniabactin synthetase==
+<StructureSection load='2n6y' size='340' side='right'caption='[[2n6y]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2n6y]] 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=2N6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N6Y FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4HH:O-[(S)-HYDROXY{[(3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-({3-OXO-3-[(2-SULFANYLETHYL)AMINO]PROPYL}AMINO)BUTYL]OXY}PHOSPHORYL]-L-SERINE'>4HH</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=2n6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6y OCA], [https://pdbe.org/2n6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n6y RCSB], [https://www.ebi.ac.uk/pdbsum/2n6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A3N4B635_YERPE A0A3N4B635_YERPE]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nonribosomal peptide synthetases (NRPSs) are microbial enzymes that produce a wealth of important natural products by condensing substrates in an assembly line manner. The proper sequence of substrates is obtained by tethering them to phosphopantetheinyl arms of holo carrier proteins (CPs) via a thioester bond. CPs in holo and substrate-loaded forms visit NRPS catalytic domains in a series of transient interactions. A lack of structural information on substrate-loaded carrier proteins has hindered our understanding of NRPS synthesis. Here, we present the first structure of an NRPS aryl carrier protein loaded with its substrate via a native thioester bond, together with the structure of its holo form. We also present the first quantification of NRPS CP backbone dynamics. Our results indicate that prosthetic moieties in both holo and loaded forms are in contact with the protein core, but they also sample states in which they are disordered and extend in solution. We observe that substrate loading induces a large conformational change in the phosphopantetheinyl arm, thereby modulating surfaces accessible for binding to other domains. Our results are discussed in the context of NRPS domain interactions.
-Authors: Goodrich, A.C., Harden, B.J., Frueh, D.P.
+Solution Structure of a Nonribosomal Peptide Synthetase Carrier Protein Loaded with Its Substrate Reveals Transient, Well-Defined Contacts.,Goodrich AC, Harden BJ, Frueh DP J Am Chem Soc. 2015 Sep 23;137(37):12100-9. doi: 10.1021/jacs.5b07772. Epub 2015 , Sep 15. PMID:26334259<ref>PMID:26334259</ref>
-Description: Solution structure of holo ArCP from yersiniabactin synthetase
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Goodrich, A.C]]
+<div class="pdbe-citations 2n6y" style="background-color:#fffaf0;"></div>
-[[Category: Harden, B.J]]
+== References ==
-[[Category: Frueh, D.P]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Yersinia pestis]]
+[[Category: Frueh DP]]
+[[Category: Goodrich AC]]
+[[Category: Harden BJ]]