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Literature DB >> 16754987

Purification, crystallization and preliminary X-ray analysis of Mycobacterium tuberculosisfolylpolyglutamate synthase (MtbFPGS).

P G Young¹, C A Smith, X Sun, E N Baker, P Metcalf.

Abstract

The gene encoding Mycobacterium tuberculosis FPGS (MtbFPGS; Rv2447c) has been cloned and the protein (51 kDa) expressed in Escherichia coli. The purified protein was crystallized either by the batch method in the presence of adenosine diphosphate (ADP) and CoCl2 or by vapour diffusion in the presence of ADP, dihydrofolate and CaCl2. X-ray diffraction data to approximately 2.0 and 2.6 A resolution were collected at the Stanford Synchrotron Radiation Laboratory (SSRL) for crystals grown under the respective conditions. Both crystals belong to the cubic space group P2(1)3, with a unit-cell parameter of 112.6 and 111.8 A, respectively. Structure determination is proceeding.

Entities: Chemical Disease Species

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Year: 2006 PMID： 16754987 PMCID： PMC2243083 DOI： 10.1107/S1744309106017180

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

12 in total

1. A flexible and economical medium-throughput strategy for protein production and crystallization.

Authors: Nicole Moreland; Rachael Ashton; Heather M Baker; Ivan Ivanovic; Sean Patterson; Vickery L Arcus; Edward N Baker; J Shaun Lott
Journal: Acta Crystallogr D Biol Crystallogr Date: 2005-09-28

Review 2. Physiology of folic acid in health and disease.

Authors: O Stanger
Journal: Curr Drug Metab Date: 2002-04 Impact factor: 3.731

Review 3. New perspectives on folate catabolism.

Authors: J R Suh; A K Herbig; P J Stover
Journal: Annu Rev Nutr Date: 2001 Impact factor: 11.848

4. Folate-binding triggers the activation of folylpolyglutamate synthetase.

Authors: X Sun; J A Cross; A L Bognar; E N Baker; C A Smith
Journal: J Mol Biol Date: 2001-07-27 Impact factor: 5.469

5. Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.

Authors: Magali Mathieu; Guy Debousker; Sophie Vincent; Fabrice Viviani; Nathalie Bamas-Jacques; Vincent Mikol
Journal: J Biol Chem Date: 2005-02-10 Impact factor: 5.157

6. Replacement of the folC gene, encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli, with genes mutagenized in vitro.

Authors: C Pyne; A L Bognar
Journal: J Bacteriol Date: 1992-03 Impact factor: 3.490

Purification, crystallization and preliminary X-ray analysis of Mycobacterium tuberculosisfolylpolyglutamate synthase (MtbFPGS).

1. A flexible and economical medium-throughput strategy for protein production and crystallization.

Review 2. Physiology of folic acid in health and disease.

Review 3. New perspectives on folate catabolism.

4. Folate-binding triggers the activation of folylpolyglutamate synthetase.

5. Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.

6. Replacement of the folC gene, encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli, with genes mutagenized in vitro.

Review 7. Folylpolyglutamate synthesis and role in the regulation of one-carbon metabolism.

8. A graphical user interface to the CCP4 program suite.

Review 9. The integration of macromolecular diffraction data.

Review 10. Scaling and assessment of data quality.

1. Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis.

2. Structures of Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP and AMPPCP.