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2pmz

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[[Image:2pmz.jpg|left|200px]]<br /><applet load="2pmz" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pmz, resolution 3.40&Aring;" />
 
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'''Archaeal RNA polymerase from Sulfolobus solfataricus'''<br />
 
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==Overview==
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==Archaeal RNA polymerase from Sulfolobus solfataricus==
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<StructureSection load='2pmz' size='340' side='right'caption='[[2pmz]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2pmz]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PMZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pmz OCA], [https://pdbe.org/2pmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pmz RCSB], [https://www.ebi.ac.uk/pdbsum/2pmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pmz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/RPOP_SULSO RPOP_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOH_SULSO RPOH_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOL_SULSO RPOL_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOA2_SULSO RPOA2_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOK_SULSO RPOK_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOA1_SULSO RPOA1_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOD_SULSO RPOD_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00320] [[https://www.uniprot.org/uniprot/RPON_SULSO RPON_SULSO]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pm/2pmz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2pmz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of each enzyme that enable it to perform domain-specific gene expression. However, the structure of archaeal RNAP has been limited to individual subunits. Here we report the first crystal structure of the archaeal RNAP from Sulfolobus solfataricus at 3.4 A resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of archaeal RNAP and provide the first experimental evidence of any RNAP possessing an iron-sulphur (Fe-S) cluster, which may play a structural role in a key subunit of RNAP assembly. The striking structural similarity between archaeal RNAP and eukaryotic RNAPII highlights the simpler archaeal RNAP as an ideal model system for dissecting the molecular basis of eukaryotic transcription.
The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of each enzyme that enable it to perform domain-specific gene expression. However, the structure of archaeal RNAP has been limited to individual subunits. Here we report the first crystal structure of the archaeal RNAP from Sulfolobus solfataricus at 3.4 A resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of archaeal RNAP and provide the first experimental evidence of any RNAP possessing an iron-sulphur (Fe-S) cluster, which may play a structural role in a key subunit of RNAP assembly. The striking structural similarity between archaeal RNAP and eukaryotic RNAPII highlights the simpler archaeal RNAP as an ideal model system for dissecting the molecular basis of eukaryotic transcription.
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==About this Structure==
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The X-ray crystal structure of RNA polymerase from Archaea.,Hirata A, Klein BJ, Murakami KS Nature. 2008 Feb 14;451(7180):851-4. Epub 2008 Jan 30. PMID:18235446<ref>PMID:18235446</ref>
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2PMZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+1002'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+A+1003'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B+2001'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+N+1001'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Residue+P+1001'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Residue+Q+1002'>AC6</scene>, <scene name='pdbsite=AC7:Mg+Binding+Site+For+Residue+Q+1003'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Residue+R+2001'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Residue+Y+1001'>AC9</scene>, <scene name='pdbsite=BC1:Zn+Binding+Site+For+Residue+Z+1001'>BC1</scene>, <scene name='pdbsite=BC2:F3s+Binding+Site+For+Residue+D+1001'>BC2</scene> and <scene name='pdbsite=BC3:F3s+Binding+Site+For+Residue+S+1001'>BC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The X-ray crystal structure of RNA polymerase from Archaea., Hirata A, Klein BJ, Murakami KS, Nature. 2008 Feb 14;451(7180):851-4. Epub 2008 Jan 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18235446 18235446]
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</div>
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<div class="pdbe-citations 2pmz" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: DNA-directed RNA polymerase]]
[[Category: DNA-directed RNA polymerase]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Sulfolobus solfataricus]]
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[[Category: Sulso]]
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[[Category: Murakami, K S.]]
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[[Category: Murakami, K S]]
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[[Category: F3S]]
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[[Category: MG]]
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[[Category: ZN]]
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[[Category: 4fe-4s cluster binding motif]]
[[Category: 4fe-4s cluster binding motif]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: translation]]
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[[Category: Translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:13 2008''
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Current revision

Archaeal RNA polymerase from Sulfolobus solfataricus

PDB ID 2pmz

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