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3tej
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEJ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">entF, b0586, JW0578 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">entF, b0586, JW0578 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tej RCSB], [http://www.ebi.ac.uk/pdbsum/3tej PDBsum]</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=3tej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tej RCSB], [http://www.ebi.ac.uk/pdbsum/3tej PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Bruner, S D | + | [[Category: Bruner, S D]] |
| - | [[Category: Liu, Y | + | [[Category: Liu, Y]] |
| - | [[Category: Zheng, T | + | [[Category: Zheng, T]] |
[[Category: Atp- binding]] | [[Category: Atp- binding]] | ||
[[Category: Carrier domain]] | [[Category: Carrier domain]] | ||
Revision as of 21:00, 24 December 2014
Crystal structure of a domain fragment involved in peptide natural product biosynthesis
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Categories: Escherichia coli | Bruner, S D | Liu, Y | Zheng, T | Atp- binding | Carrier domain | Enterobactin biosynthesis | Ion transport | Iron | Iron transport | Ligase | Multifunctional enzyme | Nonribosomal peptide | Nucleotide- binding | Phosphopantetheine | Thioesterase | Transferase | Transport
