6b6h
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | The | + | ==The cryo-EM structure of a bacterial class I transcription activation complex== |
- | + | <StructureSection load='6b6h' size='340' side='right' caption='[[6b6h]], [[Resolution|resolution]] 3.90Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6b6h]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B6H FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
- | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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='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=6b6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b6h OCA], [http://pdbe.org/6b6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b6h RCSB], [http://www.ebi.ac.uk/pdbsum/6b6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b6h ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CRP_ECO57 CRP_ECO57]] A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding to regulate transcription. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. Plays a major role in carbon catabolite repression (CCR) (By similarity). [[http://www.uniprot.org/uniprot/RPOC_ECO57 RPOC_ECO57]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOA_ECO57 RPOA_ECO57]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOB_ECO45 RPOB_ECO45]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOZ_ECO45 RPOZ_ECO45]] 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. [[http://www.uniprot.org/uniprot/RPOD_ECOLI RPOD_ECOLI]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This is the primary sigma factor of this bacterium. | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: DNA-directed RNA polymerase]] | ||
+ | [[Category: Hong, C]] | ||
[[Category: Huang, R]] | [[Category: Huang, R]] | ||
+ | [[Category: Liu, B]] | ||
+ | [[Category: Steitz, T A]] | ||
[[Category: Yu, Z]] | [[Category: Yu, Z]] | ||
- | [[Category: | + | [[Category: Camp]] |
- | [[Category: | + | [[Category: Catabolite activator protein]] |
- | [[Category: | + | [[Category: Rna polymerase]] |
+ | [[Category: Transcription]] | ||
+ | [[Category: Transcription-transferase-dna-rna complex]] |
Revision as of 07:41, 15 November 2017
The cryo-EM structure of a bacterial class I transcription activation complex
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