1HH2

Crystal structure of NusA from Thermotoga maritima

Summary for 1HH2

• Entry DOI: 10.2210/pdb1hh2/pdb
• Descriptor: N UTILIZATION SUBSTANCE PROTEIN A (2 entities in total)
• Functional Keywords: transcription regulation, termination
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 1
• Total formula weight: 37973.29

Authors

Worbs, M.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R.,Wahl, M.C. (deposition date: 2000-12-18, release date: 2001-10-19, Last modification date: 2024-05-08)

Primary citation

Worbs, M.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R.,Wahl, M.C.
An Extended RNA Binding Surface Through Arrayed S1 and Kh Domains in Transcription Factor Nusa
Mol.Cell, 7:1177-, 2001

PubMed Abstract: The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding.

PubMed: 11430821
DOI: 10.1016/S1097-2765(01)00262-3

Experimental method

X-RAY DIFFRACTION (2.1 Å)