1zyr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1zyr' size='340' side='right'caption='[[1zyr]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1zyr' size='340' side='right'caption='[[1zyr]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1zyr]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1zyr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZYR FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=STD:STREPTOLYDIGIN'>STD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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=STD:STREPTOLYDIGIN'>STD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iw7|1iw7]], [[1smy|1smy]], [[1ynj|1ynj]], [[1ynn|1ynn]], [[1k83|1k83]], [[1i6h|1i6h]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iw7|1iw7]], [[1smy|1smy]], [[1ynj|1ynj]], [[1ynn|1ynn]], [[1k83|1k83]], [[1i6h|1i6h]]</div></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zyr OCA], [https://pdbe.org/1zyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zyr RCSB], [https://www.ebi.ac.uk/pdbsum/1zyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zyr ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/RPOZ_THET8 RPOZ_THET8]] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). [[https://www.uniprot.org/uniprot/RPOA_THET8 RPOA_THET8]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOC_THET8 RPOC_THET8]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/RPOB_THET8 RPOB_THET8]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[https://www.uniprot.org/uniprot/Q5SKW1_THET8 Q5SKW1_THET8]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity).[RuleBase:RU000715] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (By similarity).[HAMAP-Rule:MF_00963] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 08:25, 10 November 2021
Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin
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Categories: DNA-directed RNA polymerase | Large Structures | Thermus thermophilus | Arnold, E | Birktoft, J J | Borukhov, S | Clark, A D | Dharia, C | Ebright, R H | Hudson, B | Ismail, S | Laptenko, O | Lee, J | Leroy, O | Mukhopadhyay, J | Napoli, A | Sarafianos, S G | Sineva, E | Tuske, S | Wang, X | Holoenzyme | Rna polymerase | Streptolydigin | Transcription | Transferase