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PDBsum entry 1l2f
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Transcription
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PDB id
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1l2f
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of nusa from thermotoga maritima and functional implication of the n-Terminal domain.
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Authors
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D.H.Shin,
H.H.Nguyen,
J.Jancarik,
H.Yokota,
R.Kim,
S.H.Kim.
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Ref.
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Biochemistry, 2003,
42,
13429-13437.
[DOI no: ]
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PubMed id
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Abstract
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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 beta-strands. This domain shows structural similarity
with one of the helical domains of sigma(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.
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