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Literature DB >> 16754988

Cloning, purification, crystallization and preliminary crystallographic analysis of SecA from Enterococcus faecalis.

Winfried Meining¹, Johannes Scheuring, Markus Fischer, Sevil Weinkauf.

Abstract

The gene coding for SecA from Enterococcus faecalis was cloned and overexpressed in Escherichia coli. In this protein, the lysine at position 6 was replaced by an asparagine in order to reduce sensitivity towards proteases. The modified protein was purified and crystallized. Crystals diffracting to 2.4 A resolution were obtained using the vapour-diffusion technique. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 A, alpha = gamma = 90.0, beta = 119.1 degrees. A selenomethionine derivative was prepared and is currently being tested in crystallization trials.

Entities: Chemical Mutation Species

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Year: 2006 PMID： 16754988 PMCID： PMC2243102 DOI： 10.1107/S1744309106017544

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

18 in total

1. Pushing the boundaries of molecular replacement with maximum likelihood.

Authors: R J Read
Journal: Acta Crystallogr D Biol Crystallogr Date: 2001-09-21

2. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase.

Authors: Vivek Sharma; Arulandu Arockiasamy; Donald R Ronning; Christos G Savva; Andreas Holzenburg; Miriam Braunstein; William R Jacobs; James C Sacchettini
Journal: Proc Natl Acad Sci U S A Date: 2003-02-26 Impact factor: 11.205

3. Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals.

Authors: Katherine A Kantardjieff; Bernhard Rupp
Journal: Protein Sci Date: 2003-09 Impact factor: 6.725

Cloning, purification, crystallization and preliminary crystallographic analysis of SecA from Enterococcus faecalis.

1. Pushing the boundaries of molecular replacement with maximum likelihood.

2. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase.

3. Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals.

Review 4. The bacterial translocase: a dynamic protein channel complex.

5. The bacterial ATPase SecA functions as a monomer in protein translocation.

6. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA.

7. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.

8. Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.

9. Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution.

10. Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli.

1. Selective photoaffinity labeling identifies the signal peptide binding domain on SecA.