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Literature DB >> 26209027

Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis.

Ramsay Macdonald^1,2, Dibyendu Sarkar³, Brendan R Amer^1,2, Robert T Clubb^4,5.

Abstract

Entities: CellLine Chemical Disease Species

Mesh：

Substances：

Year: 2015 PMID： 26209027 PMCID： PMC4714862 DOI： 10.1007/s10858-015-9965-0

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

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22 in total

1. The Xplor-NIH NMR molecular structure determination package.

Authors: Charles D Schwieters; John J Kuszewski; Nico Tjandra; G Marius Clore
Journal: J Magn Reson Date: 2003-01 Impact factor: 2.229

2. A simple method to predict protein flexibility using secondary chemical shifts.

Authors: Mark V Berjanskii; David S Wishart
Journal: J Am Chem Soc Date: 2005-11-02 Impact factor: 15.419

3. Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosis.

Authors: Shuishu Wang; Jean Engohang-Ndong; Issar Smith
Journal: Biochemistry Date: 2007-12-01 Impact factor: 3.162

4. PhoP-PhoP interaction at adjacent PhoP binding sites is influenced by protein phosphorylation.

Authors: Akesh Sinha; Sankalp Gupta; Shweta Bhutani; Anuj Pathak; Dibyendu Sarkar
Journal: J Bacteriol Date: 2007-12-07 Impact factor: 3.490

5. MOLMOL: a program for display and analysis of macromolecular structures.

Authors: R Koradi; M Billeter; K Wüthrich
Journal: J Mol Graph Date: 1996-02

6. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.

Authors: R A Laskowski; J A Rullmannn; M W MacArthur; R Kaptein; J M Thornton
Journal: J Biomol NMR Date: 1996-12 Impact factor: 2.835

7. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis.

Authors: Shaun B Walters; Eugenie Dubnau; Irina Kolesnikova; Francoise Laval; Mamadou Daffe; Issar Smith
Journal: Mol Microbiol Date: 2006-04 Impact factor: 3.501

Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis.

1. The Xplor-NIH NMR molecular structure determination package.

2. A simple method to predict protein flexibility using secondary chemical shifts.

3. Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosis.

4. PhoP-PhoP interaction at adjacent PhoP binding sites is influenced by protein phosphorylation.

5. MOLMOL: a program for display and analysis of macromolecular structures.

6. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.

7. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis.

8. An essential role for phoP in Mycobacterium tuberculosis virulence.

Review 9. PhoP, a key player in Mycobacterium tuberculosis virulence.

10. PhoP: a missing piece in the intricate puzzle of Mycobacterium tuberculosis virulence.

1. Rapid addition of unlabeled silent solubility tags to proteins using a new substrate-fused sortase reagent.

Review 2. Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.