4na2

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate

Structural highlights

4na2 is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PKSJ_BACSU Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.^[1] ^[2]

Publication Abstract from PubMed

The recently discovered trans-acyltransferase modular polyketide synthases catalyze the biosynthesis of a wide range of bioactive natural products in bacteria. Here we report the structure of the second ketosynthase from the bacillaene trans-acyltransferase polyketide synthase. This 1.95 A resolution structure provides the highest resolution view available of a modular polyketide synthase ketosynthase and reveals a flanking subdomain that is homologous to an ordered linker in cis-acyltransferase modular polyketide synthases. The structure of the cysteine-to-serine mutant of the ketosynthase acylated by its natural substrate provides high-resolution details of how a native polyketide intermediate is bound and helps explain the basis of ketosynthase substrate specificity. The substrate range of the ketosynthase was further investigated by mass spectrometry.

A Close Look at a Ketosynthase from a Trans-Acyltransferase Modular Polyketide Synthase.,Gay DC, Gay G, Axelrod AJ, Jenner M, Kohlhaas C, Kampa A, Oldham NJ, Piel J, Keatinge-Clay AT Structure. 2014 Feb 4. pii: S0969-2126(14)00008-2. doi:, 10.1016/j.str.2013.12.016. PMID:24508341^[3]

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

References

↑ Dorrestein PC, Blackhall J, Straight PD, Fischbach MA, Garneau-Tsodikova S, Edwards DJ, McLaughlin S, Lin M, Gerwick WH, Kolter R, Walsh CT, Kelleher NL. Activity screening of carrier domains within nonribosomal peptide synthetases using complex substrate mixtures and large molecule mass spectrometry. Biochemistry. 2006 Feb 14;45(6):1537-46. PMID:16460000 doi:http://dx.doi.org/10.1021/bi052333k
↑ Butcher RA, Schroeder FC, Fischbach MA, Straight PD, Kolter R, Walsh CT, Clardy J. The identification of bacillaene, the product of the PksX megacomplex in Bacillus subtilis. Proc Natl Acad Sci U S A. 2007 Jan 30;104(5):1506-9. Epub 2007 Jan 18. PMID:17234808 doi:http://dx.doi.org/10.1073/pnas.0610503104
↑ Gay DC, Gay G, Axelrod AJ, Jenner M, Kohlhaas C, Kampa A, Oldham NJ, Piel J, Keatinge-Clay AT. A Close Look at a Ketosynthase from a Trans-Acyltransferase Modular Polyketide Synthase. Structure. 2014 Feb 4. pii: S0969-2126(14)00008-2. doi:, 10.1016/j.str.2013.12.016. PMID:24508341 doi:http://dx.doi.org/10.1016/j.str.2013.12.016

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4na2"

Categories: Bacillus subtilis subsp. subtilis str. 168 | Large Structures | Gay DC | Gay GR | Keatinge-Clay AT

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4na2 is ON HOLD
+==Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate==
+<StructureSection load='4na2' size='340' side='right'caption='[[4na2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4na2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NA2 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2JF:(2S)-2-AMINO-3-OXOPROPYL+4-{[(2S)-2-HYDROXY-4-METHYLPENTANOYL]AMINO}BUTANOATE'>2JF</scene></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=4na2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na2 OCA], [https://pdbe.org/4na2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4na2 RCSB], [https://www.ebi.ac.uk/pdbsum/4na2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4na2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PKSJ_BACSU PKSJ_BACSU] Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.<ref>PMID:16460000</ref> <ref>PMID:17234808</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The recently discovered trans-acyltransferase modular polyketide synthases catalyze the biosynthesis of a wide range of bioactive natural products in bacteria. Here we report the structure of the second ketosynthase from the bacillaene trans-acyltransferase polyketide synthase. This 1.95 A resolution structure provides the highest resolution view available of a modular polyketide synthase ketosynthase and reveals a flanking subdomain that is homologous to an ordered linker in cis-acyltransferase modular polyketide synthases. The structure of the cysteine-to-serine mutant of the ketosynthase acylated by its natural substrate provides high-resolution details of how a native polyketide intermediate is bound and helps explain the basis of ketosynthase substrate specificity. The substrate range of the ketosynthase was further investigated by mass spectrometry.
-Authors: Gay, D.C., Gay, G.R., Keatinge-Clay, A.T.
+A Close Look at a Ketosynthase from a Trans-Acyltransferase Modular Polyketide Synthase.,Gay DC, Gay G, Axelrod AJ, Jenner M, Kohlhaas C, Kampa A, Oldham NJ, Piel J, Keatinge-Clay AT Structure. 2014 Feb 4. pii: S0969-2126(14)00008-2. doi:, 10.1016/j.str.2013.12.016. PMID:24508341<ref>PMID:24508341</ref>
-Description: Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4na2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
+[[Category: Large Structures]]
+[[Category: Gay DC]]
+[[Category: Gay GR]]
+[[Category: Keatinge-Clay AT]]

4na2

From Proteopedia

Current revision

Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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