1eik: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="1eik" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eik" /> '''SOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT... |
No edit summary |
||
| (20 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Solution Structure of RNA Polymerase Subunit RPB5 from Methanobacterium Thermoautotrophicum== | ||
RPB5 is an essential subunit of eukaryotic and archaeal RNA polymerases. | <StructureSection load='1eik' size='340' side='right'caption='[[1eik]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1eik]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eik OCA], [https://pdbe.org/1eik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eik RCSB], [https://www.ebi.ac.uk/pdbsum/1eik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eik ProSAT], [https://www.topsan.org/Proteins/NESGC/1eik TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RPO5_METTH RPO5_METTH] DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00025] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ei/1eik_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<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/main_output.php?pdb_ID=1eik ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
RPB5 is an essential subunit of eukaryotic and archaeal RNA polymerases. It is a proposed target for transcription activator proteins in eukaryotes, but the mechanism of interaction is not known. We have determined the solution structure of the RPB5 subunit from the thermophilic archeon, Methanobacterium thermoautotrophicum. MtRBP5 contains a four-stranded beta-sheet platform supporting two alpha-helices, one on each side of the beta-sheet, resulting in an overall mushroom shape that does not appear to have any structural homologues in the structural database. The position and conservation of charged surface residues suggests possible modes of interaction with other proteins, as well as a rationale for the thermal stability of this protein. | |||
Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum.,Yee A, Booth V, Dharamsi A, Engel A, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6311-5. PMID:10841538<ref>PMID:10841538</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1eik" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Arrowsmith CH]] | |||
[[Category: Arrowsmith | [[Category: Booth V]] | ||
[[Category: Booth | [[Category: Dharamsi A]] | ||
[[Category: Dharamsi | [[Category: Edwards AM]] | ||
[[Category: Edwards | [[Category: Engel A]] | ||
[[Category: Engel | [[Category: Yee A]] | ||
[[Category: Yee | |||
Latest revision as of 11:26, 22 May 2024
Solution Structure of RNA Polymerase Subunit RPB5 from Methanobacterium ThermoautotrophicumSolution Structure of RNA Polymerase Subunit RPB5 from Methanobacterium Thermoautotrophicum
Structural highlights
FunctionRPO5_METTH DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00025] 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 PubMedRPB5 is an essential subunit of eukaryotic and archaeal RNA polymerases. It is a proposed target for transcription activator proteins in eukaryotes, but the mechanism of interaction is not known. We have determined the solution structure of the RPB5 subunit from the thermophilic archeon, Methanobacterium thermoautotrophicum. MtRBP5 contains a four-stranded beta-sheet platform supporting two alpha-helices, one on each side of the beta-sheet, resulting in an overall mushroom shape that does not appear to have any structural homologues in the structural database. The position and conservation of charged surface residues suggests possible modes of interaction with other proteins, as well as a rationale for the thermal stability of this protein. Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum.,Yee A, Booth V, Dharamsi A, Engel A, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6311-5. PMID:10841538[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||