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2k2q

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Revision as of 14:23, 11 September 2015

complex structure of the external thioesterase of the Surfactin-synthetase with a carrier domain

Structural highlights

2k2q is a 2 chain structure with sequence from Bacillus subtilis and Brevibacillus parabrevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ron, 2gdx
Gene:	tycC (Brevibacillus parabrevis), srfAD, srfA4 (Bacillus subtilis)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Warning: this is a large structure, and loading might take a long time or not happen at all.

Function

[TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. [SRFAD_BACSU] Probable thioesterase involved in the biosynthesis of surfactin.

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) found in bacteria, fungi and plants use two different types of thioesterases for the production of highly active biological compounds. Type I thioesterases (TEI) catalyse the release step from the assembly line of the final product where it is transported from one reaction centre to the next as a thioester linked to a 4'-phosphopantetheine (4'-PP) cofactor that is covalently attached to thiolation (T) domains. The second enzyme involved in the synthesis of these secondary metabolites, the type II thioesterase (TEII), is a crucial repair enzyme for the regeneration of functional 4'-PP cofactors of holo-T domains of NRPS and PKS systems. Mispriming of 4'-PP cofactors by acetyl- and short-chain acyl-residues interrupts the biosynthetic system. This repair reaction is very important, because roughly 80% of CoA, the precursor of the 4'-PP cofactor, is acetylated in bacteria. Here we report the three-dimensional structure of a type II thioesterase from Bacillus subtilis free and in complex with a T domain. Comparison with structures of TEI enzymes shows the basis for substrate selectivity and the different modes of interaction of TEII and TEI enzymes with T domains. Furthermore, we show that the TEII enzyme exists in several conformations of which only one is selected on interaction with its native substrate, a modified holo-T domain.

Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.,Koglin A, Lohr F, Bernhard F, Rogov VV, Frueh DP, Strieter ER, Mofid MR, Guntert P, Wagner G, Walsh CT, Marahiel MA, Dotsch V Nature. 2008 Aug 14;454(7206):907-11. PMID:18704089^[1]

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

References

↑ Koglin A, Lohr F, Bernhard F, Rogov VV, Frueh DP, Strieter ER, Mofid MR, Guntert P, Wagner G, Walsh CT, Marahiel MA, Dotsch V. Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. Nature. 2008 Aug 14;454(7206):907-11. PMID:18704089 doi:nature07161

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/2k2q"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ron|2ron]], [[2gdx|2gdx]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tycC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 Brevibacillus parabrevis]), srfAD, srfA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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=2k2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2q RCSB], [http://www.ebi.ac.uk/pdbsum/2k2q 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=2k2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2q OCA], [http://pdbe.org/2k2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k2q RCSB], [http://www.ebi.ac.uk/pdbsum/2k2q PDBsum]</span></td></tr>
 </table>
+{{Large structure}}
 == Function ==
 [[http://www.uniprot.org/uniprot/TYCC_BREPA TYCC_BREPA]] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. [[http://www.uniprot.org/uniprot/SRFAD_BACSU SRFAD_BACSU]] Probable thioesterase involved in the biosynthesis of surfactin.
@@ Line 27: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2k2q" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2k2q

From Proteopedia

Revision as of 14:23, 11 September 2015

complex structure of the external thioesterase of the Surfactin-synthetase with a carrier domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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