Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold

D  Nurizzo; J P  Turkenburg; S J  Charnock; S M  Roberts; E J  Dodson; V A  McKie; E J  Taylor; H J  Gilbert; G J  Davies

doi:10.1038/nsb835

Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold

D Nurizzo, J P Turkenburg, S J Charnock, S M Roberts, E J Dodson, V A McKie, E J Taylor, H J Gilbert, G J Davies

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Cellvibrio japonicus arabinanase Arb43A hydrolyzes the -1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Angstrom resolution, reveals a five-bladed beta-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.

Original language	English
Pages (from-to)	665-668
Number of pages	4
Journal	Nature Structural Biology
Volume	9
Issue number	9
DOIs	https://doi.org/10.1038/nsb835
Publication status	Published - Sept 2002

Keywords

GLUCURONIDASE
REPLACEMENT
REFINEMENT
HYDROLASES
DIVERSITY
DOMAIN
MODE
MAPS

Access to Document

10.1038/nsb835

Cite this

@article{355f1e7bad7f4c04bf3fa0a3e49a50ae,

title = "Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold",

abstract = "Cellvibrio japonicus arabinanase Arb43A hydrolyzes the -1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Angstrom resolution, reveals a five-bladed beta-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.",

keywords = "GLUCURONIDASE, REPLACEMENT, REFINEMENT, HYDROLASES, DIVERSITY, DOMAIN, MODE, MAPS",

author = "D Nurizzo and Turkenburg, {J P} and Charnock, {S J} and Roberts, {S M} and Dodson, {E J} and McKie, {V A} and Taylor, {E J} and Gilbert, {H J} and Davies, {G J}",

year = "2002",

month = sep,

doi = "10.1038/nsb835",

language = "English",

volume = "9",

pages = "665--668",

journal = "Nature Structural Biology",

issn = "1072-8368",

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number = "9",

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TY - JOUR

T1 - Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold

AU - Nurizzo, D

AU - Turkenburg, J P

AU - Charnock, S J

AU - Roberts, S M

AU - Dodson, E J

AU - McKie, V A

AU - Taylor, E J

AU - Gilbert, H J

AU - Davies, G J

PY - 2002/9

Y1 - 2002/9

N2 - Cellvibrio japonicus arabinanase Arb43A hydrolyzes the -1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Angstrom resolution, reveals a five-bladed beta-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.

AB - Cellvibrio japonicus arabinanase Arb43A hydrolyzes the -1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Angstrom resolution, reveals a five-bladed beta-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.

KW - GLUCURONIDASE

KW - REPLACEMENT

KW - REFINEMENT

KW - HYDROLASES

KW - DIVERSITY

KW - DOMAIN

KW - MODE

KW - MAPS

U2 - 10.1038/nsb835

DO - 10.1038/nsb835

M3 - Article

SN - 1072-8368

VL - 9

SP - 665

EP - 668

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 9

ER -