Literature DB >> 1569575

Purification and crystallization of Lactobacillus casei folylpolyglutamate synthetase expressed in Escherichia coli.

V Cody1, J R Luft, W Pangborn, J Toy, A L Bognar.   

Abstract

Folylpolyglutamate synthetase (FPGS) from Lactobacillus casei has been crystallized with polyethylene glycol and acetate buffer at pH 5.0. The enzyme was obtained from Escherichia coli strain SF4 harboring the L. casei FPGS chromosomal gene on a pEMBL vector (pGT3-8.1). Crystals of the enzyme were obtained which diffract to 2.6 A resolution. The crystals are monoclinic, space group P2(1), with unit cell dimensions of a = 54.07 A, b = 45.83 A, c = 84.37 A and beta = 107.92 degrees. A unit cell contains one molecule of the 43,000 Da enzyme per asymmetric unit. A complete X-ray data set on the native crystals has been collected.

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Year:  1992        PMID: 1569575     DOI: 10.1016/0022-2836(92)90480-8

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase.

Authors:  X Sun; A L Bognar; E N Baker; C A Smith
Journal:  Proc Natl Acad Sci U S A       Date:  1998-06-09       Impact factor: 11.205

2.  Elimination of human folypolyglutamate synthetase alters programming and plasticity of somatic cells.

Authors:  Avinash C Srivastava; Yesenia Guadalupe Thompson; Jyotsana Singhal; Jordan Stellern; Anviksha Srivastava; Juan Du; Timothy R O'Connor; Arthur D Riggs
Journal:  FASEB J       Date:  2019-10-04       Impact factor: 5.834

  2 in total

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