1hh2: Difference between revisions

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[[Image:1hh2.~~jpg~~|left|200px]]

[[Image:1hh2.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA~~'''~~

===CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA===

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11430821}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11430821 is the PubMed ID number.

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==About this Structure==

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[[Category: Termination]]

[[Category: Transcription regulation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:50:23 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:10:35 2008''

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-[[Image:1hh2.jpg|left|200px]]
+{{Seed}}
+[[Image:1hh2.png|left|200px]]
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 {{STRUCTURE_1hh2|  PDB=1hh2  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11430821}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11430821 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11430821}}
 ==About this Structure==
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 [[Category: Termination]]
 [[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:50:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:10:35 2008''