2y0s: Difference between revisions

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==Crystal structure of Sulfolobus shibatae RNA polymerase in P21 space group==
==Crystal structure of Sulfolobus shibatae RNA polymerase in P21 space group==
<StructureSection load='2y0s' size='340' side='right' caption='[[2y0s]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<StructureSection load='2y0s' size='340' side='right'caption='[[2y0s]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2y0s]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_shibatae Sulfolobus shibatae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y0S FirstGlance]. <br>
<table><tr><td colspan='2'>[[2y0s]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_shibatae Saccharolobus shibatae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2y0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y0s RCSB], [http://www.ebi.ac.uk/pdbsum/2y0s PDBsum]</span></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=2y0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0s OCA], [https://pdbe.org/2y0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0s RCSB], [https://www.ebi.ac.uk/pdbsum/2y0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPO1C_SACSH RPO1C_SACSH] DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.[HAMAP-Rule:MF_00411]<ref>PMID:19419240</ref> <ref>PMID:21265742</ref> <ref>PMID:22848102</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2y0s" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[RNA polymerase|RNA polymerase]]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed RNA polymerase]]
[[Category: Large Structures]]
[[Category: Sulfolobus shibatae]]
[[Category: Saccharolobus shibatae]]
[[Category: Abrescia, N G.A]]
[[Category: Abrescia NGA]]
[[Category: Bell, S D]]
[[Category: Bell SD]]
[[Category: Mogni, M]]
[[Category: Mogni M]]
[[Category: Ondiviela, M]]
[[Category: Ondiviela M]]
[[Category: Peralta, B]]
[[Category: Peralta B]]
[[Category: Wojtas, M]]
[[Category: Wojtas M]]
[[Category: Metal-binding]]
[[Category: Nucleotidyltransferase]]
[[Category: Transcription]]
[[Category: Transferase]]

Latest revision as of 12:38, 6 November 2024

Crystal structure of Sulfolobus shibatae RNA polymerase in P21 space groupCrystal structure of Sulfolobus shibatae RNA polymerase in P21 space group

Structural highlights

2y0s is a 20 chain structure with sequence from Saccharolobus shibatae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPO1C_SACSH DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.[HAMAP-Rule:MF_00411][1] [2] [3]

Publication Abstract from PubMed

We review recent results on the complete structure of the archaeal RNAP (RNA polymerase) enzyme of Sulfolobus shibatae. We compare the three crystal forms in which this RNAP packs (space groups P212121, P21212 and P21) and provide a preliminary biophysical characterization of the newly identified 13-subunit Rpo13. The availability of different crystal forms for this RNAP allows the analysis of the packing degeneracy and the intermolecular interactions that determine this degeneracy. We observe the pivotal role played by the protruding stalk composed of subunits Rpo4 and Rpo7 in the lattice contacts. Aided by MALLS (multi-angle laser light scattering), we have initiated the biophysical characterization of the recombinantly expressed and purified subunit Rpo13, a necessary step towards the understanding of Rpo13's role in archaeal transcription.

Archaeal RNA polymerase: the influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit.,Wojtas M, Peralta B, Ondiviela M, Mogni M, Bell SD, Abrescia NG Biochem Soc Trans. 2011 Jan 19;39(1):25-30. PMID:21265742[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Korkhin Y, Unligil UM, Littlefield O, Nelson PJ, Stuart DI, Sigler PB, Bell SD, Abrescia NG. Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure. PLoS Biol. 2009 May 5;7(5):e102. PMID:19419240 doi:10.1371/journal.pbio.1000102
  2. Wojtas M, Peralta B, Ondiviela M, Mogni M, Bell SD, Abrescia NG. Archaeal RNA polymerase: the influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit. Biochem Soc Trans. 2011 Jan 19;39(1):25-30. PMID:21265742 doi:10.1042/BST0390025
  3. Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. Nucleic Acids Res. 2012 Jul 30. PMID:22848102 doi:10.1093/nar/gks692
  4. Wojtas M, Peralta B, Ondiviela M, Mogni M, Bell SD, Abrescia NG. Archaeal RNA polymerase: the influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit. Biochem Soc Trans. 2011 Jan 19;39(1):25-30. PMID:21265742 doi:10.1042/BST0390025

2y0s, resolution 3.80Å

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