1ajk

From Proteopedia

Revision as of 12:44, 30 October 2007

CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE CPA16M-84

Overview

The 1,3-1,4-beta-glucanases from Bacillus macerans and Bacillus, licheniformis, as well as related hybrid enzymes, are stable proteins, comprised of one compact jellyroll domain. Their structures are studied in, an effort to reveal the degree of redundancy to which the, three-dimensional structure of protein domains is encoded by the amino, acid sequence. For the hybrid 1,3-1,4-beta-glucanase H(A16-M), it could be, shown recently that a circular permutation of the sequence giving rise to, the variant cpA16M-59 is compatible with wildtype-like enzymatic activity, and tertiary structure (Hahn et al., Proc. Natl. Acad. Sci. USA, 91:10417-10421, 1994). Since the circular permutation yielding cpA16M-59, mimicks that found in the homologous enzyme from Fibrobacter succinogenes, the question ... [(full description)]

About this Structure

1AJK is a [Single protein] structure of sequence from [Paenibacillus macerans] with CA, PO4 and EPE as [ligands]. Active as [Licheninase], with EC number [3.2.1.73]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [OCA].

Reference

Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases., Ay J, Hahn M, Decanniere K, Piotukh K, Borriss R, Heinemann U, Proteins. 1998 Feb 1;30(2):155-67. PMID:9489923

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