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Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase.
Acta Crystallogr D Biol Crystallogr. 2004 Nov; 60(Pt 11):2031-4.AC

Abstract

Glutamate racemase (MurI, RacE; E.C.5.1.1.3) catalyses the cofactor-independent conversion of L-glutamate to D-glutamate, an essential step in the synthesis of components of the bacterial cell wall. The gene for RacE from Bacillus subtilis has been cloned and the protein expressed in Escherichia coli, purified and crystallized in the presence of L-glutamate using the hanging-drop method of vapour diffusion with diammonium tartrate as the precipitant. The crystals belong to the monoclinic space group C2, with approximate unit-cell parameters a = 133.6, b = 60.1, c = 126.2 A, beta = 117.6 degrees . Consideration of the possible values of V(M) suggests that the asymmetric unit contains either two (V(M) = 3.75 A(3) Da(-1)) or three (V(M) = 2.5 A(3) Da(-1)) subunits. The crystals diffract X-rays to at least 2.1 A resolution on a synchrotron-radiation source and are suitable for structural studies. Determination of the structure may provide insight into the molecular basis of substrate recognition and catalysis by this enzyme.

Authors+Show Affiliations

Taal MA
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
Sedelnikova SE
No affiliation info available
Ruzheinikov SN
No affiliation info available
Baker PJ
No affiliation info available
Rice DW
No affiliation info available

MeSH

Amino Acid IsomerasesBacillus subtilisChromatography, GelCrystallizationCrystallography, X-RayGene Expression

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15502318

Citation

Taal, Makie A., et al. "Expression, Purification and Preliminary X-ray Analysis of Crystals of Bacillus Subtilis Glutamate Racemase." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 11, 2004, pp. 2031-4.
Taal MA, Sedelnikova SE, Ruzheinikov SN, et al. Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2031-4.
Taal, M. A., Sedelnikova, S. E., Ruzheinikov, S. N., Baker, P. J., & Rice, D. W. (2004). Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 11), 2031-4.
Taal MA, et al. Expression, Purification and Preliminary X-ray Analysis of Crystals of Bacillus Subtilis Glutamate Racemase. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2031-4. PubMed PMID: 15502318.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase. AU - Taal,Makie A, AU - Sedelnikova,Svetlana E, AU - Ruzheinikov,Sergey N, AU - Baker,Patrick J, AU - Rice,David W, Y1 - 2004/10/20/ PY - 2004/05/12/received PY - 2004/08/26/accepted PY - 2004/10/27/pubmed PY - 2005/5/17/medline PY - 2004/10/27/entrez SP - 2031 EP - 4 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 11 N2 - Glutamate racemase (MurI, RacE; E.C.5.1.1.3) catalyses the cofactor-independent conversion of L-glutamate to D-glutamate, an essential step in the synthesis of components of the bacterial cell wall. The gene for RacE from Bacillus subtilis has been cloned and the protein expressed in Escherichia coli, purified and crystallized in the presence of L-glutamate using the hanging-drop method of vapour diffusion with diammonium tartrate as the precipitant. The crystals belong to the monoclinic space group C2, with approximate unit-cell parameters a = 133.6, b = 60.1, c = 126.2 A, beta = 117.6 degrees . Consideration of the possible values of V(M) suggests that the asymmetric unit contains either two (V(M) = 3.75 A(3) Da(-1)) or three (V(M) = 2.5 A(3) Da(-1)) subunits. The crystals diffract X-rays to at least 2.1 A resolution on a synchrotron-radiation source and are suitable for structural studies. Determination of the structure may provide insight into the molecular basis of substrate recognition and catalysis by this enzyme. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15502318/Expression_purification_and_preliminary_X_ray_analysis_of_crystals_of_Bacillus_subtilis_glutamate_racemase_ DB - PRIME DP - Unbound Medicine ER -