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1hh2

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{{STRUCTURE_1hh2| PDB=1hh2 | SCENE= }}
{{STRUCTURE_1hh2| PDB=1hh2 | SCENE= }}
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'''CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA'''
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===CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 11430821 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11430821}}
==About this Structure==
==About this Structure==
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[[Category: Termination]]
[[Category: Termination]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:10:35 2008''

Revision as of 05:10, 1 July 2008

Image:1hh2.png

Template:STRUCTURE 1hh2

CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA

Template:ABSTRACT PUBMED 11430821

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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