Crystal Structure of NusA from Thermotoga Maritima and Functional Implication of the N-Terminal Domain

Dong Hae Shin, Henry Huy Nguyen, Jaru Jancarik, Hisao Yokota, Rosalind Kim, Sung Hou Kim

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


We report the crystal structure of N-utilizing substance A protein (NusA) from Thermotoga maritima (TmNusA), a protein involved in transcriptional pausing, termination, and antitermination. TmNusA has an elongated rod-shaped structure consisting of an N-terminal domain (NTD, residues 1-132) and three RNA binding domains (RBD). The NTD consists of two subdomains, the globular head and the helical body domains, that comprise a unique three-dimensional structure that may be important for interacting with RNA polymerase. The globular head domain possesses a high content of negatively charged residues that may interact with the positively charged flaplike domain of RNA polymerase. The helical body domain is composed of a three-helix bundle that forms a hydrophobic core with the aid of two neighboring β-strands. This domain shows structural similarity with one of the helical domains of σ 70 factor from Escherichia coli. One side of the molecular surface shows positive electrostatic potential suitable for nonspecific RNA interaction. The RBD is composed of one S1 domain and two K-homology (KH) domains forming an elongated RNA binding surface. Structural comparison between TmNusA and Mycobacterium tuberculosis NusA reveals a possible hinge motion between NTD and RBD. In addition, a functional implication of the NTD in its interaction with RNA polymerase is discussed.

Original languageEnglish
Pages (from-to)13429-13437
Number of pages9
Issue number46
StatePublished - 25 Nov 2003


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