2x3j

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[[Image:2x3j.png|left|200px]]
 
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==CO-COMPLEX STRUCTURE OF ACHROMOBACTIN SYNTHETASE PROTEIN D (ACSD) WITH ATP AND N-CITRYL-ETHYLENEDIAMINE FROM PECTOBACTERIUM CHRYSANTHEMI==
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The line below this paragraph, containing "STRUCTURE_2x3j", creates the "Structure Box" on the page.
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<StructureSection load='2x3j' size='340' side='right'caption='[[2x3j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2x3j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=X3J:(2S)-2-{2-[(2-AMINOETHYL)AMINO]-2-OXOETHYL}-2-HYDROXYBUTANEDIOIC+ACID'>X3J</scene></td></tr>
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{{STRUCTURE_2x3j| PDB=2x3j | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3j OCA], [https://pdbe.org/2x3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3j RCSB], [https://www.ebi.ac.uk/pdbsum/2x3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q93AT8_DICCH Q93AT8_DICCH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Siderophores are known virulence factors, and their biosynthesis is a target for new antibacterial agents. A non-ribosomal peptide synthetase-independent siderophore biosynthetic pathway in Dickeya dadantii is responsible for production of the siderophore achromobactin. The D. dadantii achromobactin biosynthesis protein D (AcsD) enzyme has been shown to enantioselectively esterify citric acid with l-serine in the first committed step of achromobactin biosynthesis. The reaction occurs in two steps: stereospecific activation of citric acid by adenylation, followed by attack of the enzyme-bound citryl adenylate by l-serine to produce the homochiral ester. We now report a detailed characterization of the substrate profile and mechanism of the second (acyl transfer) step of AcsD enzyme. We demonstrate that the enzyme catalyzes formation of not only esters but also amides from the citryl-adenylate intermediate. We have rationalized the substrate utilization profile for the acylation reaction by determining the first X-ray crystal structure of a product complex for this enzyme class. We have identified the residues that are important for both recognition of l-serine and catalysis of ester formation. Our hypotheses were tested by biochemical analysis of various mutants, one of which shows a reversal of specificity from the wild type with respect to non-natural substrates. This change can be rationalized on the basis of our structural data. That this change in specificity is accompanied by no loss in activity suggests that AcsD and other members of the non-ribosomal peptide synthetase-independent siderophore superfamily may have biotransformation potential.
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===CO-COMPLEX STRUCTURE OF ACHROMOBACTIN SYNTHETASE PROTEIN D (ACSD) WITH ATP AND N-CITRYL-ETHYLENEDIAMINE FROM PECTOBACTERIUM CHRYSANTHEMI===
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Structural Basis for Acyl Acceptor Specificity in the Achromobactin Biosynthetic Enzyme AcsD.,Schmelz S, Botting CH, Song L, Kadi NF, Challis GL, Naismith JH J Mol Biol. 2011 Sep 23;412(3):495-504. Epub 2011 Aug 1. PMID:21835184<ref>PMID:21835184</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_21835184}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2x3j" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 21835184 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21835184}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Dickeya chrysanthemi]]
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[[2x3j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3J OCA].
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[[Category: Large Structures]]
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[[Category: Challis GL]]
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==Reference==
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[[Category: Naismith JH]]
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<ref group="xtra">PMID:021835184</ref><references group="xtra"/>
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[[Category: Schmelz S]]
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[[Category: Erwinia chrysanthemi]]
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[[Category: Challis, G L.]]
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[[Category: Naismith, J H.]]
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[[Category: Schmelz, S.]]
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[[Category: Adenylation]]
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[[Category: Alcaligin biosynthesis]]
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[[Category: Alcc]]
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[[Category: Iron acquisition]]
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[[Category: Ligase]]
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[[Category: Siderophore]]
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Current revision

CO-COMPLEX STRUCTURE OF ACHROMOBACTIN SYNTHETASE PROTEIN D (ACSD) WITH ATP AND N-CITRYL-ETHYLENEDIAMINE FROM PECTOBACTERIUM CHRYSANTHEMI

PDB ID 2x3j

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