Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound

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O'Neill, Ellis C., Stevenson, Clare E.M., Paterson, Michael J., Rejzek, Martin, Chauvin, Anne Laure, Lawson, David M. and Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275 (2015) Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound. Proteins: Structure, Function and Bioinformatics, 83 (9). pp. 1742-1749. ISSN 0887-3585

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Abstract

The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 Å resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays α-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function.

Item Type: Article
Additional Information: Publisher Copyright: © 2015 Wiley Periodicals, Inc.
Uncontrolled Keywords: e.c. 3.2.1.40,enzyme structure,flavonoid,glycosyl hydrolase family 78,rutin,α-l-rhamnosidase,structural biology,biochemistry,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:
Faculty of Science > School of Biological Sciences
Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 04 Sep 2024 13:35
Last Modified: 25 Sep 2024 18:06
URI: https://ueaeprints.uea.ac.uk/id/eprint/96536
DOI: 10.1002/prot.24807

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