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Role of invariant water molecules and water-mediated ionic interactions in D-xylose isomerase from Streptomyces rubiginosus

Dhanasekaran, V and Velmurugan, D and Kanaujia, Shankar Prasad and Sekar, K (2013) Role of invariant water molecules and water-mediated ionic interactions in D-xylose isomerase from Streptomyces rubiginosus. In: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 31 (4). pp. 376-384.

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Official URL: http://dx.doi.org/10.1080/07391102.2012.703064

Abstract

The enzyme, D-xylose isomerase (D-xylose keto-isomerase; EC 5.3.1.5) is a soluble enzyme that catalyzes the conversion of the aldo-sugar D-xylose to the keto-sugar D-xylulose. A total of 27 subunits of D-xylose isomerase from Streptomyces rubiginosus were analyzed in order to identify the invariant water molecules and their water-mediated ionic interactions. A total of 70 water molecules were found to be invariant. The structural and/or functional roles of these water molecules have been discussed. These invariant water molecules and their ionic interactions may be involved in maintaining the structural stability of the enzyme D-xylose isomerase. Fifty-eight of the 70 invariant water molecules (83%) have at least one interaction with the main chain polar atom.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to the TAYLOR & FRANCIS INC, USA.
Keywords: invariant water molecules; ion pairs; protein stability; water-mediated ionic interactions; D-xylose isomerase; Streptomyces rubiginosus
Department/Centre: Division of Interdisciplinary Research > Supercomputer Education & Research Centre
Depositing User: Francis Jayakanth
Date Deposited: 19 Apr 2013 09:00
Last Modified: 19 Apr 2013 09:00
URI: http://eprints.iisc.ac.in/id/eprint/46382

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