1pqv

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{{STRUCTURE_1pqv| PDB=1pqv | SCENE= }}
{{STRUCTURE_1pqv| PDB=1pqv | SCENE= }}
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'''RNA polymerase II-TFIIS complex'''
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===RNA polymerase II-TFIIS complex===
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==Overview==
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The transcription elongation factor TFIIS induces mRNA cleavage by enhancing the intrinsic nuclease activity of RNA polymerase (Pol) II. We have diffused TFIIS into Pol II crystals and derived a model of the Pol II-TFIIS complex from X-ray diffraction data to 3.8 A resolution. TFIIS extends from the polymerase surface via a pore to the internal active site, spanning a distance of 100 A. Two essential and invariant acidic residues in a TFIIS loop complement the Pol II active site and could position a metal ion and a water molecule for hydrolytic RNA cleavage. TFIIS also induces extensive structural changes in Pol II that would realign nucleic acids in the active center. Our results support the idea that Pol II contains a single tunable active site for RNA polymerization and cleavage, in contrast to DNA polymerases with two separate active sites for DNA polymerization and cleavage.
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(as it appears on PubMed at http://www.pubmed.gov), where 12914699 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12914699}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:52:34 2008''

Revision as of 04:52, 29 July 2008

Image:1pqv.png

Template:STRUCTURE 1pqv

RNA polymerase II-TFIIS complex

Template:ABSTRACT PUBMED 12914699

About this Structure

1PQV is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage., Kettenberger H, Armache KJ, Cramer P, Cell. 2003 Aug 8;114(3):347-57. PMID:12914699

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