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| | ==Crystal structure of Sulfolobus Cren7-dsDNA complex== | | ==Crystal structure of Sulfolobus Cren7-dsDNA complex== |
| - | <StructureSection load='3kxt' size='340' side='right' caption='[[3kxt]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3kxt' size='340' side='right'caption='[[3kxt]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3kxt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KXT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3kxt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KXT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSO6901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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]] 1.602Å</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=3kxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kxt OCA], [http://pdbe.org/3kxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kxt RCSB], [http://www.ebi.ac.uk/pdbsum/3kxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kxt 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=3kxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kxt OCA], [https://pdbe.org/3kxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kxt RCSB], [https://www.ebi.ac.uk/pdbsum/3kxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kxt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CREN7_SULSO CREN7_SULSO]] A highly abundant probable chromatin protein, it binds double-strand DNA without sequence specificity; there is approximately 1 Cren7 molecule for 12 bp of DNA. Constrains negative DNA supercoils, increases DNA stability against thermal denaturation. Binding does not require protein methylation. Binds single-strand DNA weakly.<ref>PMID:18096617</ref> | + | [https://www.uniprot.org/uniprot/CREN7_SACS2 CREN7_SACS2] A highly abundant probable chromatin protein, it binds double-strand DNA without sequence specificity; there is approximately 1 Cren7 molecule for 12 bp of DNA. Constrains negative DNA supercoils, increases DNA stability against thermal denaturation. Binding does not require protein methylation. Binds single-strand DNA weakly.<ref>PMID:18096617</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/3kxt_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/3kxt_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | + | [[Category: Large Structures]] |
| - | [[Category: Feng, Y]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Wang, J]] | + | [[Category: Feng Y]] |
| - | [[Category: Crenarchaea chromatin protein]] | + | [[Category: Wang J]] |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Minor-groove binding]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| Structural highlights
Function
CREN7_SACS2 A highly abundant probable chromatin protein, it binds double-strand DNA without sequence specificity; there is approximately 1 Cren7 molecule for 12 bp of DNA. Constrains negative DNA supercoils, increases DNA stability against thermal denaturation. Binding does not require protein methylation. Binds single-strand DNA weakly.[1]
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
Cren7 is a crenarchaeal conserved chromatin protein discovered recently. To explore the mechanism of the DNA packaging in Crenarchaeota, the crystal structure of Cren7-GCGATCGC complex has been determined and refined at 1.6 A resolution. Cren7 kinks the dsDNA sharply similar to Sul7d, another chromatin protein existing only in Sulfolobales, which reveals that the "bending and unwinding" compacting mechanism is conserved in Crenarchaeota. Significant structural differences are revealed by comparing both protein-dsDNA complexes. The kinked sites on the same dsDNA in the complexes with Sul7d and Cren7 show one base pair shift. For Cren7, fewer charged residues in the beta-barrel structural region bind to DNA, and additionally, the flexible loop L(beta3beta4) is also involved in the binding. Electrophoretic mobility shift assays indicate that loop L(beta3beta4) is essential for DNA-binding of Cren7. These differences provide insight into the functional difference of both chromatin proteins, suggesting that Cren7 may be more regulative than Sul7d in the DNA-binding affinity by the methylation in the flexible loop L(beta3beta4) in vivo.
Crystal structure of the crenarchaeal conserved chromatin protein Cren7 and double-stranded DNA complex.,Feng Y, Yao H, Wang J Protein Sci. 2010 Jun;19(6):1253-7. PMID:20512977[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo L, Feng Y, Zhang Z, Yao H, Luo Y, Wang J, Huang L. Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea. Nucleic Acids Res. 2008 Mar;36(4):1129-37. Epub 2007 Dec 20. PMID:18096617 doi:10.1093/nar/gkm1128
- ↑ Feng Y, Yao H, Wang J. Crystal structure of the crenarchaeal conserved chromatin protein Cren7 and double-stranded DNA complex. Protein Sci. 2010 Jun;19(6):1253-7. PMID:20512977 doi:10.1002/pro.385
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