5bp4: Difference between revisions
New page: '''Unreleased structure''' The entry 5bp4 is ON HOLD Authors: Herbst, D.A., Jakob, P.R., Zaehringer, F., Maier, T. Description: Enzyme ligand complex 3 [[Category: Unreleased Structure... |
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==Modifying region (DH-ER-KR) of a mycocerosic acid synthase-like (MAS-like) PKS== | |||
<StructureSection load='5bp4' size='340' side='right'caption='[[5bp4]], [[Resolution|resolution]] 3.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5bp4]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BP4 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]] 3.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5bp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp4 OCA], [https://pdbe.org/5bp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bp4 RCSB], [https://www.ebi.ac.uk/pdbsum/5bp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bp4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PKS5_MYCS2 PKS5_MYCS2] Polyketide synthase involved in the biosynthesis of 2,4-dimethyl-2-eicosenoic acid, a lipid component of the lipooligosaccharides (LOS) which are not located at the bacterial surface but rather in deeper compartments of the cell envelope of M.smegmatis.<ref>PMID:19181796</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Polyketide synthases (PKSs) are biosynthetic factories that produce natural products with important biological and pharmacological activities. Their exceptional product diversity is encoded in a modular architecture. Modular PKSs (modPKSs) catalyse reactions colinear to the order of modules in an assembly line, whereas iterative PKSs (iPKSs) use a single module iteratively as exemplified by fungal iPKSs (fiPKSs). However, in some cases non-colinear iterative action is also observed for modPKSs modules and is controlled by the assembly line environment. PKSs feature a structural and functional separation into a condensing and a modifying region as observed for fatty acid synthases. Despite the outstanding relevance of PKSs, the detailed organization of PKSs with complete fully reducing modifying regions remains elusive. Here we report a hybrid crystal structure of Mycobacterium smegmatis mycocerosic acid synthase based on structures of its condensing and modifying regions. Mycocerosic acid synthase is a fully reducing iPKS, closely related to modPKSs, and the prototype of mycobacterial mycocerosic acid synthase-like PKSs. It is involved in the biosynthesis of C20-C28 branched-chain fatty acids, which are important virulence factors of mycobacteria. Our structural data reveal a dimeric linker-based organization of the modifying region and visualize dynamics and conformational coupling in PKSs. On the basis of comparative small-angle X-ray scattering, the observed modifying region architecture may be common also in modPKSs. The linker-based organization provides a rationale for the characteristic variability of PKS modules as a main contributor to product diversity. The comprehensive architectural model enables functional dissection and re-engineering of PKSs. | |||
Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthases.,Herbst DA, Jakob RP, Zahringer F, Maier T Nature. 2016 Mar 24;531(7595):533-7. doi: 10.1038/nature16993. Epub 2016 Mar 14. PMID:26976449<ref>PMID:26976449</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5bp4" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Maier | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycolicibacterium smegmatis MC2 155]] | |||
[[Category: Herbst DA]] | |||
[[Category: Jakob PR]] | |||
[[Category: Maier T]] | |||
[[Category: Zaehringer F]] | |||