1enw: Difference between revisions

Revision as of 15:19, 2 May 2008

ELONGATION FACTOR TFIIS DOMAIN II

OverviewOverview

Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. Limited proteolytic digestion showed that yeast TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III) are required for transcription activity. The structure of domain III has been solved previously by using NMR spectroscopy. Here, we report the NMR-derived structure of domain II: a three-helix bundle built around a hydrophobic core composed largely of three tyrosines protruding from one face of the C-terminal helix. The arrangement of known inactivating mutations of TFIIS suggests that two surfaces of domain II are critical for transcription activity.

About this StructureAbout this Structure

1ENW is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Elongation factor TFIIS contains three structural domains: solution structure of domain II., Morin PE, Awrey DE, Edwards AM, Arrowsmith CH, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10604-8. PMID:8855225 Page seeded by OCA on Fri May 2 15:19:32 2008

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OCA

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 '''ELONGATION FACTOR TFIIS DOMAIN II'''
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 [[Category: Edwards, A M.]]
 [[Category: Morin, P E.]]
-[[Category: helix-bundle]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:19:32 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:06:19 2008''