1r7j

<table><tr><td colspan='2'>[[1r7j]] is a 1 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=1R7J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R7J FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sso10a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r7j OCA], [http://pdbe.org/1r7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r7j RCSB], [http://www.ebi.ac.uk/pdbsum/1r7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r7j ProSAT], [http://www.topsan.org/Proteins/SECSG/1r7j TOPSAN]</span></td></tr>

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== Publication Abstract from PubMed ==

Sso10a is a member of a group of DNA-binding proteins thought to be important in chromatin structure and regulation in the hyperthermophilic archaeon Sulfolobus solfataricus. We have determined the structure of Sso10a to 1.47A resolution directly with unlabelled native crystals by a novel approach using sulfur single-wavelength anomalous scattering (SAS) from a chromium X-ray source. The 95 amino acid residue protein contains a winged helix DNA-binding domain with an extended C-terminal alpha-helix that leads to dimerization by forming a two-stranded, antiparallel coiled-coil rod. The winged helix domains are at opposite ends of the extended coiled coil with two putative DNA-recognition helices separated by 55A and rotated by 83 degrees. Formation of stable dimers in solution is demonstrated by both analytical ultracentrifugation and differential scanning calorimetry. With a T0 of 109 degrees C, Sso10a is one of the most stable two-stranded coiled coils known. The coiled coil contains a rare aspartate residue (D69) in the normally hydrophobic d position of the heptad repeat, with two aspartate-lysine (d-g') interhelical ion pairs in the symmetrical dimer. Mutation of D69 to alanine resulted in an increase in thermal stability, indicating that destabilization resulting from the partially buried aspartate residue cannot be offset by ion pair formation. Possible DNA-binding interactions are discussed on the basis of comparisons to other winged helix proteins. The structure of Sso10a provides insight into the structures of the conserved domain represented by COG3432, a group of more than 20 hypothetical transcriptional regulators coded in the genomic sequences of both crenarchaeota and euryarchaeota.

The hyperthermophile protein Sso10a is a dimer of winged helix DNA-binding domains linked by an antiparallel coiled coil rod.,Chen L, Chen LR, Zhou XE, Wang Y, Kahsai MA, Clark AT, Edmondson SP, Liu ZJ, Rose JP, Wang BC, Meehan EJ, Shriver JW J Mol Biol. 2004 Jul 30;341(1):73-91. PMID:15312764<ref>PMID:15312764</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1r7j" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 35091]]

[[Category: Chen, L]]

[[Category: Chen, L R]]

[[Category: Clark, A T]]

[[Category: Edmondson, S P]]

[[Category: Kahsai, M A]]

[[Category: Liu, Z J]]

[[Category: Meehan, E J]]

[[Category: Rose, J P]]

[[Category: Structural genomic]]

[[Category: Shriver, J W]]

[[Category: Wang, B C]]

[[Category: Wang, Y]]

[[Category: Zhou, X E]]

[[Category: Winged helix-turn-helix]]