View source for 4na2


==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.

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>

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/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Gay DC]]
[[Category: Gay GR]]
[[Category: Keatinge-Clay AT]]