1enw: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1enw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enw OCA], [http://www.ebi.ac.uk/pdbsum/1enw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1enw RCSB]</span> | |||
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[[Category: helix-bundle]] | [[Category: helix-bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:06:19 2008'' | ||
Revision as of 20:06, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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