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| - | ==Condensing di-domain (KS-AT) of the mycocerosic acid synthase (MAS)== | + | ==Condensing di-domain (KS-AT) of a mycocerosic acid synthase-like (MAS-like) PKS== |
| - | <StructureSection load='5bp1' size='340' side='right' caption='[[5bp1]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='5bp1' size='340' side='right'caption='[[5bp1]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bp1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BP1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BP1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5bp1]] is a 1 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=5BP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BP1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bp4|5bp4]], [[5bp3|5bp3]], [[5bp2|5bp2]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.203Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mycocerosate_synthase Mycocerosate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.111 2.3.1.111] </span></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=5bp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp1 OCA], [https://pdbe.org/5bp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bp1 RCSB], [https://www.ebi.ac.uk/pdbsum/5bp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bp1 ProSAT]</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=5bp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp1 OCA], [http://pdbe.org/5bp1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bp1 RCSB], [http://www.ebi.ac.uk/pdbsum/5bp1 PDBsum]</span></td></tr> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mycocerosate synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Herbst, D A]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Jakob, R P]] | + | [[Category: Herbst DA]] |
| - | [[Category: Maier, T]] | + | [[Category: Jakob RP]] |
| - | [[Category: Zaehringer, F]] | + | [[Category: Maier T]] |
| - | [[Category: Acyltransferase]] | + | [[Category: Zaehringer F]] |
| - | [[Category: Ketosynthase]]
| + | |
| - | [[Category: Polyketide]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Etienne G, Malaga W, Laval F, Lemassu A, Guilhot C, Daffe M. Identification of the polyketide synthase involved in the biosynthesis of the surface-exposed lipooligosaccharides in mycobacteria. J Bacteriol. 2009 Apr;191(8):2613-21. doi: 10.1128/JB.01235-08. Epub 2009 Jan 30. PMID:19181796 doi:http://dx.doi.org/10.1128/JB.01235-08
- ↑ Herbst DA, Jakob RP, Zahringer F, Maier T. Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthases. Nature. 2016 Mar 24;531(7595):533-7. doi: 10.1038/nature16993. Epub 2016 Mar 14. PMID:26976449 doi:http://dx.doi.org/10.1038/nature16993
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