5bp2: Difference between revisions
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==Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 1== | ==Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 1== | ||
<StructureSection load='5bp2' size='340' side='right' caption='[[5bp2]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5bp2' size='340' side='right'caption='[[5bp2]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bp2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BP2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bp2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BP2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bp3|5bp3]], [[5bp4|5bp4]], [[5bp5|5bp5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bp3|5bp3]], [[5bp4|5bp4]], [[5bp5|5bp5]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pks5, MSMEG_4727 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=5bp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp2 OCA], [http://pdbe.org/5bp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bp2 RCSB], [http://www.ebi.ac.uk/pdbsum/5bp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bp2 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=5bp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp2 OCA], [http://pdbe.org/5bp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bp2 RCSB], [http://www.ebi.ac.uk/pdbsum/5bp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bp2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mycs2]] | |||
[[Category: Herbst, D A]] | [[Category: Herbst, D A]] | ||
[[Category: Jakob, P R]] | [[Category: Jakob, P R]] | ||
Revision as of 11:52, 11 March 2020
Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 1Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 1
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 PubMedPolyketide 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
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