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. Ravishankar (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. ISSN 0006-291X

[img] Text (Full Text)
Crystal structure of product-bound complex of UDP-N-acetyl-d-mannosamine dehydrogenase from Pyrococcus horikoshii OT3.pdf - Published Version
Restricted to Registered users only

Download (2871Kb) | Request a copy
Official URL: http://dx.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 Å. 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
Additional Information: Unmapped bibliographic data: PY - 2014/10/24/ [EPrints field already has value set] JO - Biochemical and Biophysical Research Communications [Field not mapped to EPrints]
Uncontrolled Keywords: UDP-d-ManNAcADH, UDP-d-ManNAcA, Oligomerization domain, Thermostability
Subjects: Agriculture Biological Sciences > Microbiology
University of Mysore > PG Campuses > Manasagangotri, Mysore > Agriculture Biological Sciences > Microbiology
Divisions: PG Campuses > Manasagangotri, Mysore > Microbiology
Depositing User: Ms. Swapna deepa
Date Deposited: 08 Apr 2015 10:59
Last Modified: 17 Dec 2015 11:22
URI: http://eprints.uni-mysore.ac.in/id/eprint/17678

Actions (login required)

View Item View Item