3tej

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[[Image:3tej.jpg|left|200px]]
 
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==Crystal structure of a domain fragment involved in peptide natural product biosynthesis==
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The line below this paragraph, containing "STRUCTURE_3tej", creates the "Structure Box" on the page.
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<StructureSection load='3tej' size='340' side='right'caption='[[3tej]], [[Resolution|resolution]] 1.90&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'>[[3tej]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TEJ 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]] 1.9&#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=UF0:O-[(R)-HYDROXY{[(3R)-3-HYDROXY-4-{[3-({2-[(HYDROXYACETYL)AMINO]ETHYL}AMINO)-3-OXOPROPYL]AMINO}-2,2-DIMETHYL-4-OXOBUTYL]OXY}PHOSPHORYL]-L-SERINE'>UF0</scene></td></tr>
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{{STRUCTURE_3tej| PDB=3tej | 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=3tej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tej OCA], [https://pdbe.org/3tej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tej RCSB], [https://www.ebi.ac.uk/pdbsum/3tej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tej ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENTF_ECOLI ENTF_ECOLI] Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phosphopantetheine-modified carrier domains play a central role in the template-directed, biosynthesis of several classes of primary and secondary metabolites. Fatty acids, polyketides, and nonribosomal peptides are constructed on multidomain enzyme assemblies using phosphopantetheinyl thioester-linked carrier domains to traffic and activate building blocks. The carrier domain is a dynamic component of the process, shuttling pathway intermediates to sequential enzyme active sites. Here, we report an approach to structurally fix carrier domain/enzyme constructs suitable for X-ray crystallographic analysis. The structure of a two-domain construct of Escherichia coli EntF was determined with a conjugated phosphopantetheinyl-based inhibitor. The didomain structure is locked in an active orientation relevant to the chemistry of nonribosomal peptide biosynthesis. This structure provides details into the interaction of phosphopantetheine arm with the carrier domain and the active site of the thioesterase domain.
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===Crystal structure of a domain fragment involved in peptide natural product biosynthesis===
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Structural basis for phosphopantetheinyl carrier domain interactions in the terminal module of nonribosomal peptide synthetases.,Liu Y, Zheng T, Bruner SD Chem Biol. 2011 Nov 23;18(11):1482-8. PMID:22118682<ref>PMID:22118682</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_22118682}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3tej" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 22118682 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22118682}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[3tej]] is a 2 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=3TEJ OCA].
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[[Category: Large Structures]]
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[[Category: Bruner SD]]
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==Reference==
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[[Category: Liu Y]]
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<ref group="xtra">PMID:022118682</ref><references group="xtra"/>
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[[Category: Zheng T]]
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[[Category: Escherichia coli]]
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[[Category: Bruner, S D.]]
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[[Category: Liu, Y.]]
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[[Category: Zheng, T.]]
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[[Category: Atp- binding]]
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[[Category: Carrier domain]]
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[[Category: Enterobactin biosynthesis]]
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[[Category: Ion transport]]
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[[Category: Iron]]
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[[Category: Iron transport]]
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[[Category: Ligase]]
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[[Category: Multifunctional enzyme]]
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[[Category: Nonribosomal peptide]]
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[[Category: Nucleotide- binding]]
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[[Category: Phosphopantetheine]]
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[[Category: Thioesterase]]
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[[Category: Transferase]]
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[[Category: Transport]]
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Current revision

Crystal structure of a domain fragment involved in peptide natural product biosynthesis

PDB ID 3tej

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