1enw: Difference between revisions

Revision as of 01:12, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1enw.png

Template:STRUCTURE 1enw

ELONGATION FACTOR TFIIS DOMAIN IIELONGATION FACTOR TFIIS DOMAIN II

Template:ABSTRACT PUBMED 8855225

About this StructureAbout this Structure

1ENW is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental 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 Tue Jul 1 01:11:50 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1enw.jpg|left|200px]]
+{{Seed}}
+[[Image:1enw.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1enw|  PDB=1enw  |  SCENE=  }}
-'''ELONGATION FACTOR TFIIS DOMAIN II'''
+===ELONGATION FACTOR TFIIS DOMAIN II===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8855225}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8855225 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8855225}}
 ==About this Structure==
-ENW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENW OCA].
+ENW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENW OCA].
 ==Reference==
@@ Line 27: / Line 31: @@
 [[Category: Morin, P E.]]
 [[Category: Helix-bundle]]
-''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 Tue Jul  1 01:11:50 2008''