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PDBsum entry 1hh2
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Transcription regulation
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PDB id
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1hh2
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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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An extended RNA binding surface through arrayed s1 and kh domains in transcription factor nusa.
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Authors
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M.Worbs,
G.P.Bourenkov,
H.D.Bartunik,
R.Huber,
M.C.Wahl.
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Ref.
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Mol Cell, 2001,
7,
1177-1189.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 4.
Figure 4. Domain Stacking(a) Closeup of the interactions
between S1 and KH1. The view is from the back of Figure 1b, with
S1 at the left and KH1 at the right.(b) Details of the KH1–KH2
contacts. The view is from the left in Figure 1b, with KH1
rotated to the left and KH2 to the right. Absolutely conserved
residues involved in the interactions are labeled
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Figure 5.
Figure 5. KH Arrays(a) Arrangement of the NusA KH domains
via opposite poles. The view is from the bottom right of Figure
1b.(b) Ribbon diagram of the same region with a KH1-bound RNA
hairpin rotated  vert,
similar 90° counterclockwise about the longitudinal axis.
The prime RNA binding peptides as deduced from Figure 3 are
labeled (red). Additional contacts through KH2 are in green.(c)
Crystal contacts of two NOVA KH3·RNA complexes. The
bottom KH domains in (a) and (c) are in approximately the same
orientation
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2001,
7,
1177-1189)
copyright 2001.
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