1hh2
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(New page: 200px<br /><applet load="1hh2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hh2, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 00:26, 25 November 2007
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CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA
Overview
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.
About this Structure
1HH2 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA., Worbs M, Bourenkov GP, Bartunik HD, Huber R, Wahl MC, Mol Cell. 2001 Jun;7(6):1177-89. PMID:11430821
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