Structural highlights
Function
R4MFJ2_MYCTX
Publication Abstract from PubMed
Tuberculosis caused by Mycobacterium tuberculosis is a leading cause of death world-wide. The PhoP protein is required for virulence and is part of the PhoPR two-component system that regulates gene expression. The NMR-derived solution structure of the PhoP C-terminal DNA-binding domain is reported. Residues 150 to 246 form a structured domain that contains a winged helix-turn-helix motif. We provide evidence that the transactivation loop postulated to contact RNA polymerase is partially disordered in solution, and that the polypeptide that connects the DNA-binding domain to the regulatory domain is unstructured.
Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis.,Macdonald R, Sarkar D, Amer BR, Clubb RT J Biomol NMR. 2015 Sep;63(1):111-7. doi: 10.1007/s10858-015-9965-0. Epub 2015 Jul , 25. PMID:26209027[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Macdonald R, Sarkar D, Amer BR, Clubb RT. Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis. J Biomol NMR. 2015 Sep;63(1):111-7. PMID:26209027 doi:10.1007/s10858-015-9965-0
