4YUF: Crystal Structure Of Corb

Citation:
Abstract
Corallopyronin A is a polyketide derived from the myxobacterium Corallococcus coralloides with potent antibiotic features. The gene cluster responsible for the biosynthesis of corallopyronin A has been described recently, and it was proposed that CorB acts as a ketosynthase to interconnect two polyketide chains in a rare head-to-head condensation reaction. We determined the structure of CorB, the interconnecting polyketide synthase, to high resolution and found that CorB displays a thiolase fold. Site-directed mutagenesis showed that the catalytic triad consisting of a cysteine, a histidine and an asparagine is crucial for catalysis, and that this triad shares similarities with the triad found in HMG-CoA synthases. We synthesized a substrate mimic to derivatize purified CorB and confirmed substrate attachment by ESI-MS. Structural analysis of the complex yielded an electron density-based model for the polyketide chain and showed that the unusually wide, T-shaped active site is able to accommodate two polyketides simultaneously. Our structural analysis provides a platform for understanding the unusual head-to-head polyketide-interconnecting reaction catalyzed by CorB.
PDB ID: 4YUFDownload
MMDB ID: 137811
PDB Deposition Date: 2015/3/18
Updated in MMDB: 2017/09
Experimental Method:
x-ray diffraction
Resolution: 1.54  Å
Source Organism:
Similar Structures:
Biological Unit for 4YUF: dimeric; determined by author and by software (PISA)
Molecular Components in 4YUF
Label Count Molecule
Proteins (2 molecules)
2
Corb
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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