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| | <StructureSection load='2zfw' size='340' side='right'caption='[[2zfw]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='2zfw' size='340' side='right'caption='[[2zfw]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zfw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synsp Synsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZFW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zfw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZFW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dql|2dql]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pex ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1131 SYNSP])</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=2zfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zfw OCA], [https://pdbe.org/2zfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zfw RCSB], [https://www.ebi.ac.uk/pdbsum/2zfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zfw ProSAT]</span></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=2zfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zfw OCA], [https://pdbe.org/2zfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zfw RCSB], [https://www.ebi.ac.uk/pdbsum/2zfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zfw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O66226_SYNE7 O66226_SYNE7] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synsp]] | + | [[Category: Synechococcus sp]] |
| - | [[Category: Kouyama, T]] | + | [[Category: Kouyama T]] |
| - | [[Category: Circadian clock protein]]
| + | |
| - | [[Category: Five alpha-helices + one beta-sheet]]
| + | |
| Structural highlights
Function
O66226_SYNE7
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
Pex, a clock-related protein involved in the input pathway of the cyanobacterial circadian clock system, suppresses the expression of clock gene kaiA and lengthens the circadian period. Here, we determined the crystal structure of Anabaena Pex (AnaPex; Anabaena sp. strain PCC 7120) and Synechococcus Pex (SynPex; Synechococcus sp. strain PCC 7942). Pex is a homodimer that forms a winged-helix structure. Using the DNase I protection and electrophoresis mobility shift assays on a Synechococcus kaiA upstream region, we identified a minimal 25-bp sequence that contained an imperfectly inverted repeat sequence as the Pex-binding sequence. Based on crystal structure, we predicted the amino acid residues essential for Pex's DNA-binding activity and examined the effects of various Ala-substitutions in the alpha3 helix and wing region of Pex on in vitro DNA-binding activity and in vivo rhythm functions. Mutant AnaPex proteins carrying a substitution in the wing region displayed no specific DNA-binding activity, whereas those carrying a substitution in the alpha3 helix did display specific binding activity. But the latter were less thermostable than wild-type AnaPex and their in vitro functions were defective. We concluded that Pex binds a kaiA upstream DNA sequence via its wing region and that its alpha3 helix is probably important to its stability.
Functionally important structural elements of the cyanobacterial clock-related protein Pex.,Kurosawa S, Murakami R, Onai K, Morishita M, Hasegawa D, Iwase R, Uzumaki T, Hayashi F, Kitajima-Ihara T, Sakata S, Murakami M, Kouyama T, Ishiura M Genes Cells. 2009 Jan;14(1):1-16. Epub 2008 Nov 21. PMID:19032344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kurosawa S, Murakami R, Onai K, Morishita M, Hasegawa D, Iwase R, Uzumaki T, Hayashi F, Kitajima-Ihara T, Sakata S, Murakami M, Kouyama T, Ishiura M. Functionally important structural elements of the cyanobacterial clock-related protein Pex. Genes Cells. 2009 Jan;14(1):1-16. Epub 2008 Nov 21. PMID:19032344 doi:10.1111/j.1365-2443.2008.01245.x
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