4xhc

Publication Abstract from PubMed

The crystal structure of the GH78 family alpha-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 A 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 alpha-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function. This article is protected by copyright. All rights reserved.

Crystal structure of a novel two domain GH78 family alpha-rhamnosidase from Klebsiella oxytoca with rhamnose bound.,O'Neill EC, Stevenson CE, Paterson MJ, Rejzek M, Chauvin AL, Lawson DM, Field RA Proteins. 2015 Apr 3. doi: 10.1002/prot.24807. PMID:25846411^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.