4ZAH

Crystal structure of sugar aminotransferase WecE with External Aldimine VII from Escherichia coli K-12

Replaces:  4WFP

Summary for 4ZAH

• Entry DOI: 10.2210/pdb4zah/pdb
• Related: 4PIW
• Descriptor: dTDP-4-amino-4,6-dideoxygalactose transaminase, [[(2R,3S,5R)-5-[5-methyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4S,5R,6R)-6-methyl-5-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3,4-bis(oxidanyl)oxan-2-yl] hydrogen phosphate (3 entities in total)
• Functional Keywords: sugar aminotransferase, structural genomics, psi-biology, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, transferase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 8
• Total formula weight: 359149.90

Authors

Wang, F.,Singh, S.,Cao, H.,Xu, W.,Miller, M.D.,Thorson, J.S.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2015-04-13, release date: 2015-04-29, Last modification date: 2023-09-27)

Primary citation

Wang, F.,Singh, S.,Xu, W.,Helmich, K.E.,Miller, M.D.,Cao, H.,Bingman, C.A.,Thorson, J.S.,Phillips, G.N.
Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases.
Acs Chem.Biol., 10:2048-2056, 2015

PubMed Abstract: Sugar aminotransferases (SATs) are an important class of tailoring enzymes that catalyze the 5'-pyridoxal phosphate (PLP)-dependent stereo- and regiospecific installation of an amino group from an amino acid donor (typically L-Glu or L-Gln) to a corresponding ketosugar nucleotide acceptor. Herein we report the strategic structural study of two homologous C4 SATs (Micromonospora echinospora CalS13 and Escherichia coli WecE) that utilize identical substrates but differ in their stereochemistry of aminotransfer. This study reveals for the first time a new mode of SAT sugar nucleotide binding and, in conjunction with previously reported SAT structural studies, provides the basis from which to propose a universal model for SAT stereo- and regiochemical control of amine installation. Specifically, the universal model put forth highlights catalytic divergence to derive solely from distinctions within nucleotide sugar orientation upon binding within a relatively fixed SAT active site where the available ligand bound structures of the three out of four representative C3 and C4 SAT examples provide a basis for the overall model. Importantly, this study presents a new predictive model to support SAT functional annotation, biochemical study and rational engineering.

PubMed: 26023720
DOI: 10.1021/acschembio.5b00244

Experimental method

X-RAY DIFFRACTION (2.24 Å)