1K0R

Crystal Structure of Mycobacterium tuberculosis NusA

Summary for 1K0R

• Entry DOI: 10.2210/pdb1k0r/pdb
• Descriptor: NusA, SULFATE ION (3 entities in total)
• Functional Keywords: two component arrangement, s1 domain, two k-homology domains., structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transcription
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 80120.21

Authors

Gopal, B.,Haire, L.F.,Gamblin, S.J.,Dodson, E.J.,Lane, A.N.,Papavinasasundaram, K.G.,Colston, M.J.,Dodson, G.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2001-09-20, release date: 2001-12-21, Last modification date: 2024-02-07)

Primary citation

Gopal, B.,Haire, L.F.,Gamblin, S.J.,Dodson, E.J.,Lane, A.N.,Papavinasasundaram, K.G.,Colston, M.J.,Dodson, G.
Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution.
J.Mol.Biol., 314:1087-1095, 2001

PubMed Abstract: Mycobacterium tuberculosis is the cause of tuberculosis in humans, a disease that affects over a one-third of the world's population. This slow-growing pathogen has only one ribosomal RNA operon, thus making its transcriptional apparatus a fundamentally interesting target for drug discovery. NusA binds to RNA polymerase and modulates several of the ribosomal RNA transcriptional processes. Here, we report the crystal structure of NusA, and reveal that the molecule consists of four domains. They are organised as two distinct entities. The N-terminal domain (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329) consisting of a ribosomal S1 protein domain followed by two K homology domains. The S1 and KH domains are tightly integrated together to form an extensive RNA-binding structure, but are flexibly tethered to the N-terminal domain. The molecule's surfaces and architecture provide insights into RNA and polymerase interactions and the mechanism of pause site discrimination. They also allow us to rationalize certain termination-defective and cold shock-sensitive mutations in the nusA gene that have been studied in Escherichia coli.

PubMed: 11743725
DOI: 10.1006/jmbi.2000.5144

Experimental method

X-RAY DIFFRACTION (1.7 Å)