Crystal structure of a bacterial chitinase at 2.3 A resolution


Perrakis, A, Tews, I, Dauter, Z, Oppenheim, A B, Chet, I, Wilson, K S and Vorgias, C E (1994) Crystal structure of a bacterial chitinase at 2.3 A resolution Structure, 2, (12), pp. 1169-1180. (doi:10.1016/S0969-2126(94)00119-7). (PMID:7704527).

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Description/Abstract

The reaction mechanism seems to be similar to that of lysozyme and most other glycosylhydrolases, i.e. general acid-base catalysis. The role of the amino-terminal domain could not be identified, but it has similarities to the fibronectin III domain. This domain may possibly facilitate the interaction of chitinase A with chitin.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1016/S0969-2126(94)00119-7
ISSNs: 0969-2126 (print)
Related URLs:
Subjects: Q Science > QD Chemistry
Organisations: Centre for Biological Sciences
ePrint ID: 200661
Date :
Date Event
15 December 1994Published
Date Deposited: 02 Nov 2011 14:39
Last Modified: 18 Apr 2017 01:25
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/200661

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