1eo0

From Proteopedia

(Difference between revisions)

Revision as of 03:48, 6 September 2017

CONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70

Structural highlights

1eo0 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1enw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[TFS2_YEAST] Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

TFIIS is a transcription elongation factor that consists of three domains. We have previously solved the structures of domains II and III, which stimulate arrested polymerase II elongation complexes in order to resume transcription. Domain I is conserved in evolution from yeast to human species and is homologous to the transcription factors elongin A and CRSP70. Domain I also interacts with the transcriptionally active RNA polymerase II holoenzyme and therefore, may have a function unrelated to the previously described transcription elongation activity of TFIIS. We have solved the structure of domain I of yeast TFIIS using NMR spectroscopy. Domain I is a compact four-helix bundle that is structurally independent of domains II and III of the TFIIS. Using the yeast structure as a template, we have modeled the homologous domains from elongin A and CRSP70 and identified a conserved positively charged patch on the surface of all three proteins, which may be involved in conserved functional interactions with the transcriptional machinery.

Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70.,Booth V, Koth CM, Edwards AM, Arrowsmith CH J Biol Chem. 2000 Oct 6;275(40):31266-8. PMID:10811649^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Booth V, Koth CM, Edwards AM, Arrowsmith CH. Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70. J Biol Chem. 2000 Oct 6;275(40):31266-8. PMID:10811649 doi:http://dx.doi.org/10.1074/jbc.M002595200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eo0"

@@ Line 1: / Line 1: @@
 ==CONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70==
 <StructureSection load='1eo0' size='340' side='right' caption='[[1eo0]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1eo0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EO0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1eo0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EO0 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1enw|1enw]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo0 OCA], [http://pdbe.org/1eo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eo0 RCSB], [http://www.ebi.ac.uk/pdbsum/1eo0 PDBsum], [http://www.topsan.org/Proteins/NESGC/1eo0 TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo0 OCA], [http://pdbe.org/1eo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eo0 RCSB], [http://www.ebi.ac.uk/pdbsum/1eo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eo0 ProSAT], [http://www.topsan.org/Proteins/NESGC/1eo0 TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eo0 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Arrowsmith, C H]]
 [[Category: Booth, V]]

1eo0

From Proteopedia

Revision as of 03:48, 6 September 2017

CONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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