3qqc: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain== | ==Crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain== | ||
<StructureSection load='3qqc' size='340' side='right' caption='[[3qqc]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='3qqc' size='340' side='right' caption='[[3qqc]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qqc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3qqc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QQC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF1563 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF1563 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), PF1990 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), PF0255 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=3qqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qqc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qqc RCSB], [http://www.ebi.ac.uk/pdbsum/3qqc PDBsum]</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=3qqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qqc OCA], [http://pdbe.org/3qqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qqc RCSB], [http://www.ebi.ac.uk/pdbsum/3qqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qqc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Line 17: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3qqc" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Line 24: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Pyrfu]] | ||
[[Category: Martinez-Rucobo, F W]] | [[Category: Martinez-Rucobo, F W]] | ||
[[Category: Chimera protein]] | [[Category: Chimera protein]] |
Revision as of 23:17, 4 August 2016
Crystal structure of archaeal Spt4/5 bound to the RNAP clamp domainCrystal structure of archaeal Spt4/5 bound to the RNAP clamp domain
Structural highlights
Function[SPT4_PYRFU] Stimulates transcription elongation.[1] [2] [SPT5_PYRFU] Stimulates transcription elongation.[3] [4] Publication Abstract from PubMedRelated RNA polymerases (RNAPs) carry out cellular gene transcription in all three kingdoms of life. The universal conservation of the transcription machinery extends to a single RNAP-associated factor, Spt5 (or NusG in bacteria), which renders RNAP processive and may have arisen early to permit evolution of long genes. Spt5 associates with Spt4 to form the Spt4/5 heterodimer. Here, we present the crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain, which forms one side of the RNAP active centre cleft. The structure revealed a conserved Spt5-RNAP interface and enabled modelling of complexes of Spt4/5 counterparts with RNAPs from all kingdoms of life, and of the complete yeast RNAP II elongation complex with bound Spt4/5. The N-terminal NGN domain of Spt5/NusG closes the RNAP active centre cleft to lock nucleic acids and render the elongation complex stable and processive. The C-terminal KOW1 domain is mobile, but its location is restricted to a region between the RNAP clamp and wall above the RNA exit tunnel, where it may interact with RNA and/or other factors. Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity.,Martinez-Rucobo FW, Sainsbury S, Cheung AC, Cramer P EMBO J. 2011 Mar 8. PMID:21386817[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|