5x4z: Difference between revisions
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<StructureSection load='5x4z' size='340' side='right'caption='[[5x4z]], [[Resolution|resolution]] 7.80Å' scene=''> | <StructureSection load='5x4z' size='340' side='right'caption='[[5x4z]], [[Resolution|resolution]] 7.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5x4z]] is a | <table><tr><td colspan='2'>[[5x4z]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_phaffii_CBS_7435 Komagataella phaffii CBS 7435] and [https://en.wikipedia.org/wiki/Komagataella_phaffii_GS115 Komagataella phaffii GS115]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X4Z FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 7.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5x4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x4z OCA], [https://pdbe.org/5x4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x4z RCSB], [https://www.ebi.ac.uk/pdbsum/5x4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x4z ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/C4R4Y0_KOMPG C4R4Y0_KOMPG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Komagataella phaffii CBS 7435]] | ||
[[Category: | [[Category: Komagataella phaffii GS115]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ehara | [[Category: Ehara H]] | ||
[[Category: Sekine | [[Category: Sekine S]] | ||
[[Category: Umehara | [[Category: Umehara T]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 10:44, 17 October 2024
RNA Polymerase II from Komagataella Pastoris (Type-1 crystal)RNA Polymerase II from Komagataella Pastoris (Type-1 crystal)
Structural highlights
FunctionC4R4Y0_KOMPG DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] Publication Abstract from PubMedRNA polymerase II (Pol II) is a 12-subunit protein complex that conducts the transcription of mRNA and some small RNAs. In this work, the crystal structure of Pol II from the methylotropic yeast Komagataella pastoris (Pichia pastoris) was determined. While the structure is highly homologous to that of Pol II from the budding yeast Saccharomyces cerevisiae, the stalk and clamp modules of the K. pastoris Pol II displayed large inward rotations, closing the central cleft to a greater extent than in the known S. cerevisiae Pol II structures. The conformational differences reflect the inherent flexibilities of the stalk and the clamp, as additional low-resolution structures of K. pastoris Pol II in different crystal forms revealed diverse stalk and clamp orientations. Comparisons with other eukaryotic/archaeal RNA polymerase structures in the Protein Data Bank revealed the distributions of the stalk and clamp orientations. The conformational plasticity should be essential for transcriptional functions and binding various regulatory factors. Crystal structure of RNA polymerase II from Komagataella pastoris.,Ehara H, Umehara T, Sekine SI, Yokoyama S Biochem Biophys Res Commun. 2017 May 27;487(2):230-235. doi:, 10.1016/j.bbrc.2017.04.039. Epub 2017 Apr 12. PMID:28412353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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