5isx: Difference between revisions
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==Structure of the holo PCP-E didomain of the gramicidin S synthetase A== | |||
<StructureSection load='5isx' size='340' side='right' caption='[[5isx]], [[Resolution|resolution]] 2.33Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5isx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5isw|5isw]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolyzing) Phenylalanine racemase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.11 5.1.1.11] </span></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=5isx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isx OCA], [http://pdbe.org/5isx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isx RCSB], [http://www.ebi.ac.uk/pdbsum/5isx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/GRSA_BREBE GRSA_BREBE]] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nonribosomal peptide synthetases are large, complex multidomain enzymes responsible for the biosynthesis of a wide range of peptidic natural products. Inherent to synthetase chemistry is the thioester templated mechanism that relies on protein/protein interactions and interdomain dynamics. Several questions related to structure and mechanism remain to be addressed, including the incorporation of accessory domains and intermodule interactions. The inclusion of nonproteinogenic d-amino acids into peptide frameworks is a common and important modification for bioactive nonribosomal peptides. Epimerization domains, embedded in nonribosomal peptide synthetases assembly lines, catalyze the l- to d-amino acid conversion. Here we report the structure of the epimerization domain/peptidyl carrier protein didomain construct from the first module of the cyclic peptide antibiotic gramicidin synthetase. Both holo (phosphopantethiene post-translationally modified) and apo structures were determined, each representing catalytically relevant conformations of the two domains. The structures provide insight into domain-domain recognition, substrate delivery during the assembly line process, in addition to the structural organization of homologous condensation domains, canonical players in all synthetase modules. | |||
Interdomain and Intermodule Organization in Epimerization Domain Containing Nonribosomal Peptide Synthetases.,Chen WH, Li K, Guntaka NS, Bruner SD ACS Chem Biol. 2016 Jun 24. PMID:27294598<ref>PMID:27294598</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5isx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bruner, S D]] | |||
[[Category: Chen, W H]] | |||
[[Category: Li, K]] | |||
[[Category: Epimerization domain]] | |||
[[Category: Gramicidin s]] | |||
[[Category: Isomerase]] | |||
[[Category: Nrp]] | |||
Revision as of 10:25, 13 July 2016
Structure of the holo PCP-E didomain of the gramicidin S synthetase A
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