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Crystal structure of a novel two domain GH78 family α-rhamnosidase from
DOI:
10.1002/prot.24807
PMID:
25846411
Authors:
Ellis C.
O'Neill
(John Innes Centre)
,
Clare
Stevenson
(John Innes Centre)
,
Michael J.
Paterson
(John Innes Centre)
,
Martin
Rejzek
(John Innes Centre)
,
Anne-Laure
Chauvin
(Laboratorio Nacional De Genómica Para La Biodiversidad (Langebio))
,
David
Lawson
(John Innes Centre)
,
Robert A.
Field
(John Innes Centre)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Proteins: Structure, Function, And Bioinformatics
, VOL 83 (9)
, PAGES 1742 - 1749
State:
Published (Approved)
Published:
September 2015
Diamond Proposal Number(s):
7641
Open Access
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. Proteins 2015; 83:1742–1749. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.
Journal Keywords: α-L-Rhamnosidase; Glycosyl Hydrolase Family 78; Enzyme Structure; Flavonoid; Rutin; E.C. 3.2.1.40
Subject Areas:
Biology and Bio-materials
Instruments:
I04-1-Macromolecular Crystallography (fixed wavelength)
,
I24-Microfocus Macromolecular Crystallography
Added On:
20/11/2015 14:49
Discipline Tags:
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)