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

Ellis C. O'Neill; Clare E.M. Stevenson; Michael J. Paterson; Martin Rejzek; Anne Laure Chauvin; David M. Lawson; Robert A. Field

doi:10.1002/prot.24807

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

Ellis C. O'Neill, Clare E.M. Stevenson, Michael J. Paterson, Martin Rejzek, Anne Laure Chauvin, David M. Lawson, Robert A. Field

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

35 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1742-1749
Number of pages	8
Journal	Proteins: Structure, Function and Bioinformatics
Volume	83
Issue number	9
DOIs	https://doi.org/10.1002/prot.24807
Publication status	Published - 1 Sep 2015

Keywords

E.C. 3.2.1.40
Enzyme structure
Flavonoid
Glycosyl hydrolase family 78
Rutin
α-l-rhamnosidase

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

abstract = "The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 {\AA} 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.",

keywords = "E.C. 3.2.1.40, Enzyme structure, Flavonoid, Glycosyl hydrolase family 78, Rutin, α-l-rhamnosidase",

author = "O'Neill, {Ellis C.} and Stevenson, {Clare E.M.} and Paterson, {Michael J.} and Martin Rejzek and Chauvin, {Anne Laure} and Lawson, {David M.} and Field, {Robert A.}",

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year = "2015",

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doi = "10.1002/prot.24807",

language = "English",

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Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound. / O'Neill, Ellis C.; Stevenson, Clare E.M.; Paterson, Michael J.; Rejzek, Martin; Chauvin, Anne Laure; Lawson, David M.; Field, Robert A.

In: Proteins: Structure, Function and Bioinformatics, Vol. 83, No. 9, 01.09.2015, p. 1742-1749.

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

TY - JOUR

T1 - Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound

AU - O'Neill, Ellis C.

AU - Stevenson, Clare E.M.

AU - Paterson, Michael J.

AU - Rejzek, Martin

AU - Chauvin, Anne Laure

AU - Lawson, David M.

AU - Field, Robert A.

PY - 2015/9/1

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AB - 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.

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KW - Enzyme structure

KW - Flavonoid

KW - Glycosyl hydrolase family 78

KW - Rutin

KW - α-l-rhamnosidase

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JO - Proteins-Structure Function and Bioinformatics

JF - Proteins-Structure Function and Bioinformatics

SN - 0887-3585

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ER -

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

Abstract

Keywords

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