Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants

P M Chandra; J A Brannigan; A Prabhune; A Pundle; J P Turkenburg; G G Dodson; C G Suresh

doi:10.1107/S1744309104031227

Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants

P M Chandra, J A Brannigan, A Prabhune, A Pundle, J P Turkenburg, G G Dodson, C G Suresh

Chemistry

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

Abstract

The crystallization of three catalytically inactive mutants of penicillin Vacylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide threedimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme.

Original language	English
Pages (from-to)	124-127
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	61
Issue number	1
DOIs	https://doi.org/10.1107/S1744309104031227
Publication status	Published - Jan 2005

Bibliographical note

Keywords

N-TERMINAL NUCLEOPHILE
CEPHALOSPORIN ACYLASE
BACILLUS-SPHAERICUS
CRYSTAL-STRUCTURES
HYDROLASE FAMILY
ACTIVATION
ACID
INSIGHTS
REVEALS
ENZYME

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branniganja17.pdf

http://www.iucr.org/cgi-bin/paper?za5079

Cite this

Chandra, P. M., Brannigan, J. A., Prabhune, A., Pundle, A., Turkenburg, J. P., Dodson, G. G., & Suresh, C. G. (2005). Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(1), 124-127. https://doi.org/10.1107/S1744309104031227

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title = "Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants",

abstract = "The crystallization of three catalytically inactive mutants of penicillin Vacylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide threedimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme.",

keywords = "N-TERMINAL NUCLEOPHILE, CEPHALOSPORIN ACYLASE, BACILLUS-SPHAERICUS, CRYSTAL-STRUCTURES, HYDROLASE FAMILY, ACTIVATION, ACID, INSIGHTS, REVEALS, ENZYME",

author = "Chandra, {P M} and Brannigan, {J A} and A Prabhune and A Pundle and Turkenburg, {J P} and Dodson, {G G} and Suresh, {C G}",

note = "Copyright {\textcopyright} 2005 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?za5079",

year = "2005",

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Chandra, PM, Brannigan, JA, Prabhune, A, Pundle, A, Turkenburg, JP, Dodson, GG & Suresh, CG 2005, 'Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 61, no. 1, pp. 124-127. https://doi.org/10.1107/S1744309104031227

Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants. / Chandra, P M; Brannigan, J A; Prabhune, A et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 1, 01.2005, p. 124-127.

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

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AU - Dodson, G G

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KW - HYDROLASE FAMILY

KW - ACTIVATION

KW - ACID

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KW - ENZYME

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