1hh2
From Proteopedia
(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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| - | [[Image:1hh2.jpg|left|200px]]<br /><applet load="1hh2" size=" | + | [[Image:1hh2.jpg|left|200px]]<br /><applet load="1hh2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hh2, resolution 2.1Å" /> | caption="1hh2, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA'''<br /> | '''CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Thermotoga maritima NusA, a transcription factor | + | 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== | ==About this Structure== | ||
| - | 1HH2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http:// | + | 1HH2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Bartunik, H | + | [[Category: Bartunik, H D.]] |
| - | [[Category: Bourenkov, G | + | [[Category: Bourenkov, G P.]] |
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
| - | [[Category: Wahl, M | + | [[Category: Wahl, M C.]] |
[[Category: Worbs, M.]] | [[Category: Worbs, M.]] | ||
[[Category: termination]] | [[Category: termination]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:11 2008'' |
Revision as of 11:01, 21 February 2008
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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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