3rg2
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Structure of a two-domain NRPS fusion protein containing the EntE adenylation domain and EntB aryl-carrier protein from enterobactin biosynthesis== | |
| - | + | <StructureSection load='3rg2' size='340' side='right' caption='[[3rg2]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | { | + | <table><tr><td colspan='2'>[[3rg2]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RG2 FirstGlance]. <br> |
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=SVS:5-DEOXY-5-({[2-(2-HYDROXYPHENYL)ETHYL]SULFONYL}AMINO)ADENOSINE'>SVS</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0594, entE, entE and entB, JW0586 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3rg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rg2 RCSB], [http://www.ebi.ac.uk/pdbsum/3rg2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nonribosomal peptide synthetases (NRPSs) are modular proteins that produce peptide antibiotics and siderophores. These enzymes act as catalytic assembly lines where substrates, covalently bound to integrated carrier domains, are delivered to adjacent catalytic domains. The carrier domains are initially loaded by adenylation domains, which use two distinct conformations to catalyze sequentially the adenylation of the substrate and the thioesterification of the pantetheine cofactor. We have used a mechanism-based inhibitor to determine the crystal structure of an engineered adenylation-carrier domain protein illustrating the intermolecular interaction between the adenylation and carrier domains. This structure enabled directed mutations to improve the interaction between nonnative partner proteins. Comparison with prior NRPS adenylation domain structures provides insights into the assembly line dynamics of these modular enzymes. | ||
| - | + | Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains.,Sundlov JA, Shi C, Wilson DJ, Aldrich CC, Gulick AM Chem Biol. 2012 Feb 24;19(2):188-98. PMID:22365602<ref>PMID:22365602</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | < | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Gulick, A M | + | [[Category: Gulick, A M]] |
| - | [[Category: Sundlov, J A | + | [[Category: Sundlov, J A]] |
[[Category: 4'phosphopantetheinylation 4'pp cofactor]] | [[Category: 4'phosphopantetheinylation 4'pp cofactor]] | ||
[[Category: Adenylate-forming enzyme]] | [[Category: Adenylate-forming enzyme]] | ||
Revision as of 09:26, 4 January 2015
Structure of a two-domain NRPS fusion protein containing the EntE adenylation domain and EntB aryl-carrier protein from enterobactin biosynthesis
| |||||||||||
