Conserved structural features and sequence patterns in the GroES fold family.

Taneja, Bhupesh and Mande, S C (1999) Conserved structural features and sequence patterns in the GroES fold family. Protein engineering, 12 (10). pp. 815-8. ISSN 0269-2139

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Abstract

An irregular, all beta-class of proteins, comprising members of the chaperonin-10, quinone oxidoreductase, glucose dehydrogenase and alcohol dehydrogenase families has earlier been classified as the GroES fold. In this communication, we present an extensive analysis of sequences and three dimensional structures of proteins belonging to this family. The individual protein structures can be superposed within 1.6 A for more than 60 structurally equivalent residues. The comparisons show a highly conserved hydrophobic core and conservation of a few key residues. A glycyl-aspartate dipeptide is suggested as being critical for the maintenance of the GroES fold. One of the surprising findings of the study is the non-conservative nature of Ile to Leu mutations in the protein core, although Ile to Val mutations are found to occur frequently.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Oxford University Press
Uncontrolled Keywords:	alcohol dehydrogenaseβ-barrelchaperonin-10GroES-fold
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	03 Jan 2012 16:49
Last Modified:	09 Jan 2015 11:13
URI:	http://crdd.osdd.net/open/id/eprint/338

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