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1vgl

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Revision as of 22:56, 10 September 2015

Crystal structure of tetrameric KaiB from T.elongatus BP-1

Structural highlights

1vgl is a 4 chain structure with sequence from Theeb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

KaiB is a component of the circadian clock molecular machinery in cyanobacteria, which are the simplest organisms that exhibit circadian rhythms. Here we report the x-ray crystal structure of KaiB from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. The KaiB crystal diffracts at a resolution of 2.6 A and includes four subunits organized as a dimer of dimers, each composed of two non-equivalent subunits. The overall shape of the tetramer is an elongated hexagonal plate, with a single positively charged cleft flanked by two negatively charged ridges whose surfaces includes several terminal chains. Site-directed mutagenesis of Synechococcus KaiB confirmed that alanine substitution of residues Lys-11 or Lys-43 in the cleft, or deletion of C-terminal residues 95-108, which forms part of the ridges, strongly weakens in vivo circadian rhythms. Characteristics of KaiB deduced from the x-ray crystal structure were also confirmed by physicochemical measurements of KaiB in solution. These data suggest that the positively charged cleft and flanking negatively charged ridges in KaiB are essential for the biological function of KaiB in the circadian molecular machinery in cyanobacteria.

Functionally important substructures of circadian clock protein KaiB in a unique tetramer complex.,Iwase R, Imada K, Hayashi F, Uzumaki T, Morishita M, Onai K, Furukawa Y, Namba K, Ishiura M J Biol Chem. 2005 Dec 30;280(52):43141-9. Epub 2005 Oct 13. PMID:16227211^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Iwase R, Imada K, Hayashi F, Uzumaki T, Morishita M, Onai K, Furukawa Y, Namba K, Ishiura M. Functionally important substructures of circadian clock protein KaiB in a unique tetramer complex. J Biol Chem. 2005 Dec 30;280(52):43141-9. Epub 2005 Oct 13. PMID:16227211 doi:http://dx.doi.org/10.1074/jbc.M503360200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vgl"

@@ Line 2: / Line 2: @@
 <StructureSection load='1vgl' size='340' side='right' caption='[[1vgl]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vgl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_elongatus_bp-1 Thermosynechococcus elongatus bp-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VGL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vgl]] is a 4 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=1VGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VGL FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=1vgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vgl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vgl RCSB], [http://www.ebi.ac.uk/pdbsum/1vgl PDBsum]</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=1vgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vgl OCA], [http://pdbe.org/1vgl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vgl RCSB], [http://www.ebi.ac.uk/pdbsum/1vgl PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KAIB_SYNEL KAIB_SYNEL]] 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 (By similarity).
+[[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]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1vgl" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Thermosynechococcus elongatus bp-1]]
+[[Category: Theeb]]
 [[Category: Hayashi, F]]
 [[Category: Imada, K]]

1vgl

From Proteopedia

Revision as of 22:56, 10 September 2015

Crystal structure of tetrameric KaiB from T.elongatus BP-1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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