5jyt

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Current revision (10:12, 14 June 2023) (edit) (undo)
 
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==NMR structure of foldswitch-stablized KaiB from Thermosynechococcus elongatus==
==NMR structure of foldswitch-stablized KaiB from Thermosynechococcus elongatus==
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<StructureSection load='5jyt' size='340' side='right'caption='[[5jyt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5jyt' size='340' side='right'caption='[[5jyt]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JYT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JYT FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jyv|5jyv]], [[5jyu|5jyu]]</td></tr>
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</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=5jyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jyt OCA], [https://pdbe.org/5jyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jyt RCSB], [https://www.ebi.ac.uk/pdbsum/5jyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jyt ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kaiB, tlr0482 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</td></tr>
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<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=5jyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jyt OCA], [http://pdbe.org/5jyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jyt RCSB], [http://www.ebi.ac.uk/pdbsum/5jyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jyt ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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]
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[https://www.uniprot.org/uniprot/KAIB_THEVB KAIB_THEVB] Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria (PubMed:24112939, PubMed:16227211, PubMed:28302851). Its composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to KaiC yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA (PubMed:28302851). KaiB switches to a thioredoxin-like fold (KaiB(fs)) in complex with KaiC (PubMed:26113641, PubMed:28302851). KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from the CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (PubMed:28302851).<ref>PMID:16227211</ref> <ref>PMID:24112939</ref> <ref>PMID:26113641</ref> <ref>PMID:28302851</ref> A metamorphic protein which reversibly switches between an inactive tetrameric fold and a rare, thioredoxin-like monomeric fold (KaiB(fs)). KaiB(fs) binds phospho-KaiC, KaiA and CikA. KaiA and CikA compete for binding to KaiB(fs), and KaiB(fs) and SasA compete for binding to KaiC, thus the clock oscillator and output signal pathway are tightly coupled.[HAMAP-Rule:MF_01835]<ref>PMID:26113641</ref> <ref>PMID:28302851</ref>
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<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]]
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[[Category: Theeb]]
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[[Category: Thermosynechococcus vestitus BP-1]]
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[[Category: LiWang, A L]]
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[[Category: LiWang AL]]
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[[Category: Tseng, R D]]
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[[Category: Tseng RD]]
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[[Category: Circadian clock]]
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[[Category: Metamorphic protein]]
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[[Category: Sigaling protein]]
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Current revision

NMR structure of foldswitch-stablized KaiB from Thermosynechococcus elongatus

PDB ID 5jyt

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