1hmj: Difference between revisions
New page: left|200px<br /><applet load="1hmj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmj" /> '''SOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT... |
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== | ==SOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT H== | ||
The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly | <StructureSection load='1hmj' size='340' side='right'caption='[[1hmj]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMJ 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=1hmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmj OCA], [https://pdbe.org/1hmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmj RCSB], [https://www.ebi.ac.uk/pdbsum/1hmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RPO5_METJA RPO5_METJA] DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | |||
== 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/hm/1hmj_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=1hmj ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed beta sheet that is flanked on one side by three short helices. The dominant feature is beta-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold. | |||
RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes.,Thiru A, Hodach M, Eloranta JJ, Kostourou V, Weinzierl RO, Matthews S J Mol Biol. 1999 Apr 9;287(4):753-60. PMID:10191143<ref>PMID:10191143</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hmj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Eloranta J]] | |||
[[Category: Eloranta | [[Category: Hodach M]] | ||
[[Category: Hodach | [[Category: Kostourou V]] | ||
[[Category: Kostourou | [[Category: Thiru A]] | ||
[[Category: Thiru | [[Category: Weinzierl R]] | ||
[[Category: Weinzierl | |||
Latest revision as of 02:33, 28 December 2023
SOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT HSOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT H
Structural highlights
FunctionRPO5_METJA DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. 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 PubMedThe archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed beta sheet that is flanked on one side by three short helices. The dominant feature is beta-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold. RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes.,Thiru A, Hodach M, Eloranta JJ, Kostourou V, Weinzierl RO, Matthews S J Mol Biol. 1999 Apr 9;287(4):753-60. PMID:10191143[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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