5afq
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Crystal structure of RPC62 - RPC32 beta== |
| + | <StructureSection load='5afq' size='340' side='right' caption='[[5afq]], [[Resolution|resolution]] 7.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5afq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=5afq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afq OCA], [http://pdbe.org/5afq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5afq RCSB], [http://www.ebi.ac.uk/pdbsum/5afq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transcription initiation by eukaryotic RNA polymerase (Pol) III relies on the subcomplex RPC62/RPC39/RPC32. Two distinct isoforms of RPC32 are encoded in the human genome. RPC32alpha expression is highly regulated and found only in stem cells and transformed cells, whereas RPC32beta is ubiquitously expressed in tissues. Here we identify a core-interacting domain of RPC32 sufficient for the interaction with RPC62. We present the crystal structure of a complex of RPC62 and the RPC32beta core domain. RPC32beta associates with the extended winged helix 1 and 2 and the coiled coil domain of RPC62 qualifying RPC32 as a molecular bridge in between RPC62 domains. The RPC62-RPC32 complex fit into EM data suggests a bi-functional role for RPC32 through interactions with the largest Pol III subunit and through solvent exposed residues. RPC32 positioning into Pol III suggests that subunit-specific contacts at the surface of the Pol III holoenzyme are critical for its function. | ||
| - | + | Structural analysis of human RPC32beta-RPC62 complex.,Boissier F, Dumay-Odelot H, Teichmann M, Fribourg S J Struct Biol. 2015 Sep 21. pii: S1047-8477(15)30059-9. doi:, 10.1016/j.jsb.2015.09.004. PMID:26394183<ref>PMID:26394183</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5afq" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Fribourg, S]] | [[Category: Fribourg, S]] | ||
| + | [[Category: Human rna polymerase iii]] | ||
| + | [[Category: Replication]] | ||
Revision as of 13:42, 7 October 2015
Crystal structure of RPC62 - RPC32 beta
| |||||||||||
