Crystal structure of product-bound complex of UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3

Pampa, K. J. and Lokanath, N. K. and Girish, T. U. and Kunishima, N. and Rai, V. R. (2014) Crystal structure of product-bound complex of UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3. Biochemical and Biophysical Research Communications, 453 (3). pp. 662-667.

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Official URL: https://doi.org/10.1016/j.bbrc.2014.10.010

Abstract

UDP-N-acetyl-d-mannosamine dehydrogenase (UDP-d-ManNAcDH) belongs to UDP-glucose/GDP-mannose dehydrogenase family and catalyzes Uridine-diphospho-N-acetyl-d-mannosamine (UDP-d-ManNAc) to Uridine-diphospho-N-acetyl-d-mannosaminuronic acid (UDP-d-ManNAcA) through twofold oxidation of NAD+. In order to reveal the structural features of the Pyrococcus horikoshii UDP-d-ManNAcADH, we have determined the crystal structure of the product-bound enzyme by X-ray diffraction to resolution of 1.55 A�. The protomer folds into three distinct domains; nucleotide binding domain (NBD), substrate binding domain (SBD) and oligomerization domain (OD, involved in the dimerization). The clear electron density of the UDP-d-ManNAcA is observed and the residues binding are identified for the first time. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product is directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. In addition, the structural parameters responsible for thermostability and oligomerization of the three dimensional structure are analyzed.

Item Type: Article
Uncontrolled Keywords: Article, nonhuman, unclassified drug, X ray diffraction, chemical structure, chemistry, metabolism, enzymology, crystal structure, Crystallography, X ray crystallography, X-Ray, protein purification, sequence alignment, electron, crystallization, thermostability, Models, Molecular, binding site, Protein Conformation, oxidoreductase, Binding Sites, Carbohydrate Dehydrogenases, oligomerization, protein conformation, Pyrococcus horikoshii, UDP n acetyl dextro mannosamine dehydrogenase, UDP-N-acetylmannosamine dehydrogenase
Subjects: B Life Science > Microbiology
D Physical Science > Physics
Divisions: Department of > Microbiology
Department of > Physics
Depositing User: Arshiya Kousar
Date Deposited: 03 Sep 2019 05:18
Last Modified: 03 Sep 2019 05:18
URI: http://eprints.uni-mysore.ac.in/id/eprint/4287

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