|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4r55' size='340' side='right'caption='[[4r55]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4r55' size='340' side='right'caption='[[4r55]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r55]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R55 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r55]] is a 3 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=4R55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R55 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lwh|3lwh]], [[3lwi|3lwi]], [[4r56|4r56]]</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]] 1.8Å</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 SACS2])</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=4r55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r55 OCA], [https://pdbe.org/4r55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r55 RCSB], [https://www.ebi.ac.uk/pdbsum/4r55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r55 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=4r55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r55 OCA], [http://pdbe.org/4r55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r55 RCSB], [http://www.ebi.ac.uk/pdbsum/4r55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r55 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 == |
| Line 24: |
Line 23: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sacs2]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Chen, Y Y]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Gong, Y]] | + | [[Category: Chen YY]] |
| - | [[Category: Huang, L]] | + | [[Category: Gong Y]] |
| - | [[Category: Li, H B]] | + | [[Category: Huang L]] |
| - | [[Category: Zhang, Z F]] | + | [[Category: Li HB]] |
| - | [[Category: Beta-sheet]]
| + | [[Category: Zhang ZF]] |
| - | [[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
Sulfolobus synthesizes large amounts of small chromatin proteins Cren7 and Sul7d. The two proteins share overall structural similarity, but differ distinctly in the DNA-binding region between beta3- and beta4-strands. While Sul7d possesses a hinge of two amino acid residues, Cren7 contains a flexible seven-residue loop (loop beta3-beta4) in the region. Here, we report the role of loop beta3-beta4 in the interaction of Cren7 with duplex DNA. We show that all residues with a large side chain on the loop, i.e., Pro30, Lys31, Arg33 and Lys34, contributed significantly to the binding of Cren7 to DNA. The three basic amino acids affected the ability of Cren7 to constrain negative DNA supercoils in a residue number-dependent manner. The crystal structure of a complex between a mutant Cren7 protein (GR) with loop beta3-beta4 replaced by two residues (Gly and Arg) to mimic the hinge at the corresponding position in Sul7d and an 8-bp dsDNA has been determined. Structural comparison between the GR-DNA and Cren7-DNA complexes shows that GR resembles Sul7d more than Cren7 in DNA-binding size and in the effect on the width of the major groove of DNA and the pattern of DNA bending. However, GR induces smaller DNA curvature than Sul7d. Our results suggest that Cren7 and Sul7d package chromosomal DNA in a slightly different fashion, presumably permitting different chromosomal accessibility by proteins functioning in DNA transactions.
Insights into the interaction between Cren7 and DNA: the role of loop beta3-beta4.,Zhang Z, Gong Y, Chen Y, Li H, Huang L Extremophiles. 2015 Mar;19(2):395-406. doi: 10.1007/s00792-014-0725-y. Epub 2015 , Jan 3. PMID:25555709[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, Gong Y, Chen Y, Li H, Huang L. Insights into the interaction between Cren7 and DNA: the role of loop beta3-beta4. Extremophiles. 2015 Mar;19(2):395-406. doi: 10.1007/s00792-014-0725-y. Epub 2015 , Jan 3. PMID:25555709 doi:http://dx.doi.org/10.1007/s00792-014-0725-y
|
