5itj

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==The structure of histone-like protein==
==The structure of histone-like protein==
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<StructureSection load='5itj' size='340' side='right' caption='[[5itj]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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<StructureSection load='5itj' size='340' side='right'caption='[[5itj]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5itj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5itj]] is a 2 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=5ITJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ITJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itm|5itm]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5itj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itj OCA], [http://pdbe.org/5itj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5itj RCSB], [http://www.ebi.ac.uk/pdbsum/5itj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5itj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5itj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itj OCA], [https://pdbe.org/5itj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5itj RCSB], [https://www.ebi.ac.uk/pdbsum/5itj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5itj ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0E3K9N8_SACSO A0A0E3K9N8_SACSO]
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The Sso7c4 from Sulfolobus solfataricus forms a dimer, which is believed to function as a chromosomal protein involved in genomic DNA compaction and gene regulation. Here, we present the crystal structure of wild-type Sso7c4 at a high resolution of 1.63 A, showing that the two basic C-termini are disordered. Based on the fluorescence polarization (FP) binding assay, two arginine pairs, R11/R22' and R11'/R22, on the top surface participate in binding DNA. As shown in electron microscopy (EM) images, wild-type Sso7c4 compacts DNA through bridging and bending interactions, whereas the binding of C-terminally truncated proteins rigidifies and opens DNA molecules, and no compaction of the DNA occurs. Moreover, the FP, EM and fluorescence resonance energy transfer (FRET) data indicated that the two basic and flexible C-terminal arms of the Sso7c4 dimer play a crucial role in binding and bending DNA. Sso7c4 has been classified as a repressor-like protein because of its similarity to Escherichia coli Ecrep 6.8 and Ecrep 7.3 as well as Agrobacterium tumefaciens ACCR in amino acid sequence. Based on these data, we proposed a model of the Sso7c4-DNA complex using a curved DNA molecule in the catabolite activator protein-DNA complex. The DNA end-to-end distance measured with FRET upon wild-type Sso7c4 binding is almost equal to the distance measured in the model, which supports the fidelity of the proposed model. The FRET data also confirm the EM observation showing that the binding of wild-type Sso7c4 reduces the DNA length while the C-terminal truncation does not. A functional role for Sso7c4 in the organization of chromosomal DNA and/or the regulation of gene expression through bridging and bending interactions is suggested.
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The Arginine Pairs and C-Termini of the Sso7c4 from Sulfolobus solfataricus Participate in Binding and Bending DNA.,Lin BL, Chen CY, Huang CH, Ko TP, Chiang CH, Lin KF, Chang YC, Lin PY, Tsai HG, Wang AH PLoS One. 2017 Jan 9;12(1):e0169627. doi: 10.1371/journal.pone.0169627., eCollection 2017. PMID:28068385<ref>PMID:28068385</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5itj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chang, Y C]]
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[[Category: Large Structures]]
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[[Category: Chen, C Y]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Chiang, C H]]
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[[Category: Chang YC]]
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[[Category: Huang, C H]]
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[[Category: Chen CY]]
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[[Category: Ko, T P]]
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[[Category: Chiang CH]]
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[[Category: Lin, B L]]
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[[Category: Huang CH]]
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[[Category: Lin, K F]]
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[[Category: Ko TP]]
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[[Category: Lin, P Y]]
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[[Category: Lin BL]]
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[[Category: Tsai, H H.G]]
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[[Category: Lin KF]]
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[[Category: Wang, A H.J]]
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[[Category: Lin PY]]
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[[Category: Complex]]
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[[Category: Tsai HHG]]
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[[Category: Dna binding protein]]
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[[Category: Wang AHJ]]
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[[Category: Dna-binding fold]]
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[[Category: Histone-like protein]]
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Current revision

The structure of histone-like protein

PDB ID 5itj

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