3KG7

Dehydratase domain from CurH module of Curacin polyketide synthase

Summary for 3KG7

• Entry DOI: 10.2210/pdb3kg7/pdb
• Related: 3KG6 3KG8 3KG9
• Descriptor: CurH (2 entities in total)
• Functional Keywords: polyketide synthase, double hotdog fold, dehydratase, lyase
• Biological source: Lyngbya majuscula
• Total number of polymer chains: 4
• Total formula weight: 131792.88

Authors

Akey, D.L.,Smith, J.L. (deposition date: 2009-10-28, release date: 2010-01-19, Last modification date: 2024-10-09)

Primary citation

Akey, D.L.,Razelun, J.R.,Tehranisa, J.,Sherman, D.H.,Gerwick, W.H.,Smith, J.L.
Crystal Structures of Dehydratase Domains from the Curacin Polyketide Biosynthetic Pathway.
Structure, 18:94-105, 2010

PubMed Abstract: Modular polyketide synthases (PKS) make novel natural products through a series of preprogrammed chemical steps catalyzed by an assembly line of multidomain modules. Each assembly-line step involves unique extension and modification reactions, resulting in tremendous diversity of polyketide products. Dehydratase domains catalyze formation of an alpha,beta-double bond in the nascent polyketide intermediate. We present crystal structures of the four dehydratase domains from the curacin A PKS. The catalytic residues and substrate binding site reside in a tunnel within a single monomer. The positions of the catalytic residues and shape of the substrate tunnel explain how chirality of the substrate hydroxyl group may determine the configuration of the product double bond. Access to the active site may require opening the substrate tunnel, forming an open trench. The arrangement of monomers within the dimer is consistent among PKS dehydratases and differs from that seen in the related mammalian fatty acid synthases.

PubMed: 20152156
DOI: 10.1016/j.str.2009.10.018

Experimental method

X-RAY DIFFRACTION (2.77 Å)