5jwo: Difference between revisions

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<StructureSection load='5jwo' size='340' side='right'caption='[[5jwo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='5jwo' size='340' side='right'caption='[[5jwo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5jwo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JWO FirstGlance]. <br>
<table><tr><td colspan='2'>[[5jwo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JWO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jwq|5jwq]], [[5jwr|5jwr]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kaiC, tlr0483 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB]), kaiB, tlr0482 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</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=5jwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jwo OCA], [https://pdbe.org/5jwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jwo RCSB], [https://www.ebi.ac.uk/pdbsum/5jwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jwo ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5jwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jwo OCA], [http://pdbe.org/5jwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jwo RCSB], [http://www.ebi.ac.uk/pdbsum/5jwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jwo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KAIC_THEEB KAIC_THEEB]] Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction (By similarity).[HAMAP-Rule:MF_01836] [[http://www.uniprot.org/uniprot/KAIB_THEEB KAIB_THEEB]] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-non-specific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it decreases the phosphorylation status of KaiC. It has no effect on KaiC by itself, but instead needs the presence of both KaiA and KaiC, suggesting that it acts by antagonizing the interaction between KaiA and KaiC.[HAMAP-Rule:MF_01835]
[https://www.uniprot.org/uniprot/KAIC_THEVB KAIC_THEVB] Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Thermosynechococcus vestitus BP-1]]
[[Category: Theeb]]
[[Category: Chang Y]]
[[Category: Chang, Y]]
[[Category: Chavan A]]
[[Category: Chavan, A]]
[[Category: Goularte NF]]
[[Category: Goularte, N F]]
[[Category: Heilser J]]
[[Category: Heilser, J]]
[[Category: LiWang A]]
[[Category: LiWang, A]]
[[Category: Luu J]]
[[Category: Luu, J]]
[[Category: Partch CL]]
[[Category: Partch, C L]]
[[Category: Tripathi S]]
[[Category: Tripathi, S]]
[[Category: Tseng R]]
[[Category: Tseng, R]]
[[Category: Foldswitch]]
[[Category: Transcription regulator]]
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