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| | ==The crystal structure of Cren7 mutant L28V in complex with dsDNA== | | ==The crystal structure of Cren7 mutant L28V in complex with dsDNA== |
| - | <StructureSection load='5wvy' size='340' side='right' caption='[[5wvy]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5wvy' size='340' side='right'caption='[[5wvy]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wvy]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WVY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wvy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WVY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wvw|5wvw]], [[5wvz|5wvz]], [[5wwc|5wwc]]</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">creN7, SSO6901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</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=5wvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvy OCA], [https://pdbe.org/5wvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wvy RCSB], [https://www.ebi.ac.uk/pdbsum/5wvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvy ProSAT]</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=5wvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvy OCA], [http://pdbe.org/5wvy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wvy RCSB], [http://www.ebi.ac.uk/pdbsum/5wvy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvy 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sulso]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, Y Y]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Dong, Y H]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Gong, Y]] | + | [[Category: Chen YY]] |
| - | [[Category: Huang, L]] | + | [[Category: Dong YH]] |
| - | [[Category: Wang, L]] | + | [[Category: Gong Y]] |
| - | [[Category: Zhang, Z F]] | + | [[Category: Huang L]] |
| - | [[Category: Zhao, M H]] | + | [[Category: Wang L]] |
| - | [[Category: Beta-sheet]] | + | [[Category: Zhang ZF]] |
| - | [[Category: Crenarchaeal chromatin protein]] | + | [[Category: Zhao MH]] |
| - | [[Category: Dna binding]]
| + | |
| - | [[Category: Dna binding 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]
Publication Abstract from PubMed
Crenarchaeal chromatin protein Cren7 binds double-stranded DNA in the minor groove, introducing a sharp single-step DNA kink. The side chain of Leu28, a residue conserved among all Cren7 homologues, intercalates into the kink DNA step. In this study, we replaced Leu28 with a residue containing a hydrophobic side chain of different sizes (i.e., L28A, L28V, L28I, L28M and L28F). Both the stability of the Cren7-DNA complex and the ability of Cren7 to constrain DNA supercoils correlated well with the size of the intercalated side chain. Structural analysis shows that L28A induces a kink (~43o), nearly as sharp as that produced by wild-type Cren7 (~48o), in the bound DNA despite the lack of side chain intercalation. L28F inserts a large hydrophobic side chain deep into the DNA step, but introduces a smaller kink (~39o) than that formed by the wild-type protein (~50o). Mutation of Leu28 into methionine yields two protein conformers differing in loop beta3-beta4 orientation as well as DNA binding surface and DNA geometry in the protein-DNA structure. Our results indicate that side chain intercalation is not directly responsible for DNA kinking or bending by Cren7, but plays a critical role in the stabilization of the Cren7-DNA complex. In addition, the flexibility of loop beta3-beta4 in Cren7, as revealed in the crystal structure of L28M-DNA, may serve a role in the modulation of chromosomal organization and function in the cell.
Roles of Leu28 side chain intercalation in the interaction between Cren7 and DNA.,Zhang Z, Zhao M, Wang L, Chen Y, Dong Y, Gong Y, Huang L Biochem J. 2017 Apr 4. pii: BCJ20170036. doi: 10.1042/BCJ20170036. PMID:28377493[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
- ↑ Zhang Z, Zhao M, Wang L, Chen Y, Dong Y, Gong Y, Huang L. Roles of Leu28 side chain intercalation in the interaction between Cren7 and DNA. Biochem J. 2017 Apr 4. pii: BCJ20170036. doi: 10.1042/BCJ20170036. PMID:28377493 doi:http://dx.doi.org/10.1042/BCJ20170036
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