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2roq

From Proteopedia

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Solution Structure of the thiolation-thioesterase di-domain of enterobactin synthetase component F

Structural highlights

2roq is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) produce numerous secondary metabolites with various therapeutic/antibiotic properties. Like fatty acid synthases (FAS), these enzymes are organized in modular assembly lines in which each module, made of conserved domains, incorporates a given monomer unit into the growing chain. Knowledge about domain or module interactions may enable reengineering of this assembly line enzymatic organization and open avenues for the design of new bioactive compounds with improved therapeutic properties. So far, little structural information has been available on how the domains interact and communicate. This may be because of inherent interdomain mobility hindering crystallization, or because crystallized molecules may not represent the active domain orientations. In solution, the large size and internal dynamics of multidomain fragments (>35 kilodaltons) make structure determination by nuclear magnetic resonance a challenge and require advanced technologies. Here we present the solution structure of the apo-thiolation-thioesterase (T-TE) di-domain fragment of the Escherichia coli enterobactin synthetase EntF NRPS subunit. In the holoenzyme, the T domain carries the growing chain tethered to a 4'-phosphopantetheine whereas the TE domain catalyses hydrolysis and cyclization of the iron chelator enterobactin. The T-TE di-domain forms a compact but dynamic structure with a well-defined domain interface; the two active sites are at a suitable distance for substrate transfer from T to TE. We observe extensive interdomain and intradomain motions for well-defined regions and show that these are modulated by interactions with proteins that participate in the biosynthesis. The T-TE interaction described here provides a model for NRPS, PKS and FAS function in general as T-TE-like di-domains typically catalyse the last step in numerous assembly-line chain-termination machineries.

Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase.,Frueh DP, Arthanari H, Koglin A, Vosburg DA, Bennett AE, Walsh CT, Wagner G Nature. 2008 Aug 14;454(7206):903-6. PMID:18704088^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Frueh DP, Arthanari H, Koglin A, Vosburg DA, Bennett AE, Walsh CT, Wagner G. Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase. Nature. 2008 Aug 14;454(7206):903-6. PMID:18704088 doi:10.1038/nature07162

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2roq"

@@ Line 1: / Line 1: @@
 ==Solution Structure of the thiolation-thioesterase di-domain of enterobactin synthetase component F==
-<StructureSection load='2roq' size='340' side='right' caption='[[2roq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2roq' size='340' side='right'caption='[[2roq]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2roq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ROQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2roq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ROQ FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ent ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2roq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2roq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2roq RCSB], [http://www.ebi.ac.uk/pdbsum/2roq PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2roq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2roq OCA], [https://pdbe.org/2roq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2roq RCSB], [https://www.ebi.ac.uk/pdbsum/2roq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2roq ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[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).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/2roq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/2roq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2roq ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2roq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 29: / Line 33: @@
 </StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Arthanari, H.]]
+[[Category: Large Structures]]
-[[Category: Bennett, A E.]]
+[[Category: Arthanari H]]
-[[Category: Frueh, D P.]]
+[[Category: Bennett AE]]
-[[Category: Koglin, A.]]
+[[Category: Frueh DP]]
-[[Category: Vosburg, D A.]]
+[[Category: Koglin A]]
-[[Category: Wagner, G.]]
+[[Category: Vosburg DA]]
-[[Category: Walsh, C T.]]
+[[Category: Wagner G]]
-[[Category: Alpha/beta-hydrolase]]
+[[Category: Walsh CT]]
-[[Category: Didomain]]
-[[Category: Enterobactin]]
-[[Category: Enterobactin biosynthesis]]
-[[Category: Entf]]
-[[Category: Ion transport]]
-[[Category: Iron]]
-[[Category: Iron transport]]
-[[Category: Ligase]]
-[[Category: Multifunctional enzyme]]
-[[Category: Non-ribosomal peptide synthetase]]
-[[Category: Nrp]]
-[[Category: Pcp]]
-[[Category: Peptidyl carrier protein]]
-[[Category: Phosphopantetheine]]
-[[Category: T-te]]
-[[Category: Thioesterase]]
-[[Category: Thiolation domain]]
-[[Category: Transferase]]
-[[Category: Transport]]

2roq

From Proteopedia

Current revision

Solution Structure of the thiolation-thioesterase di-domain of enterobactin synthetase component F

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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