View source for 5erb


==Ketosynthase from module 5 of the bacillaene synthase from Bacillus amyloliquefaciens FZB42==
<StructureSection load='5erb' size='340' side='right'caption='[[5erb]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5erb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ERB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ERB 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]] 4.2&#8491;</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=5erb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5erb OCA], [https://pdbe.org/5erb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5erb RCSB], [https://www.ebi.ac.uk/pdbsum/5erb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5erb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1RS72_BACAM Q1RS72_BACAM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Polyketides such as the clinically-valuable antibacterial agent mupirocin are constructed by architecturally-sophisticated assembly lines known as trans-acyltransferase polyketide synthases. Organelle-sized megacomplexes composed of several copies of trans-acyltransferase polyketide synthase assembly lines have been observed by others through transmission electron microscopy to be located at the Bacillus subtilis plasma membrane, where the synthesis and export of the antibacterial polyketide bacillaene takes place. In this work we analyze ten crystal structures of trans-acyltransferase polyketide synthases ketosynthase domains, seven of which are reported here for the first time, to characterize a motif capable of zippering assembly lines into a megacomplex. While each of the three-helix LINKS (Laterally-INteracting Ketosynthase Sequence) motifs is observed to similarly dock with a spatially-reversed copy of itself through hydrophobic and ionic interactions, the amino acid sequences of this motif are not conserved. Such a code is appropriate for mediating homotypic contacts between assembly lines to ensure the ordered self-assembly of a noncovalent, yet tightly-knit, enzymatic network. LINKS-mediated lateral interactions would also have the effect of bolstering the vertical association of the polypeptides that comprise a polyketide synthase assembly line.

The LINKS motif zippers trans-acyltransferase polyketide synthase assembly lines into a biosynthetic megacomplex.,Gay DC, Wagner DT, Meinke JL, Zogzas CE, Gay GR, Keatinge-Clay AT J Struct Biol. 2016 Mar;193(3):196-205. doi: 10.1016/j.jsb.2015.12.011. Epub 2015, Dec 23. PMID:26724270<ref>PMID:26724270</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5erb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Large Structures]]
[[Category: Gay DC]]
[[Category: Keatinge-Clay AT]]
[[Category: Meinke J]]
[[Category: Wagner DT]]