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5bp3

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Revision as of 09:36, 2 January 2017

Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 2

Structural highlights

5bp3 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5bp4, 5bp5, 5bp2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5bp3"

@@ Line 1: / Line 1: @@
-==Dehydratase domain (DH) of the mycocerosic acid synthase (MAS), crystal form 2==
+==Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 2==
 <StructureSection load='5bp3' size='340' side='right' caption='[[5bp3]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bp4|5bp4]], [[5bp5|5bp5]], [[5bp2|5bp2]]</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=5bp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp3 OCA], [http://pdbe.org/5bp3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bp3 RCSB], [http://www.ebi.ac.uk/pdbsum/5bp3 PDBsum]</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=5bp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bp3 OCA], [http://pdbe.org/5bp3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bp3 RCSB], [http://www.ebi.ac.uk/pdbsum/5bp3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bp3 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==

5bp3

From Proteopedia

Revision as of 09:36, 2 January 2017

Dehydratase domain (DH) of a mycocerosic acid synthase-like (MAS-like) PKS, crystal form 2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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