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From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q5SI36_THET8 Q5SI36_THET8] | [https://www.uniprot.org/uniprot/Q5SI36_THET8 Q5SI36_THET8] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The gene encoding TTHA1544 is a singleton found in the Thermus thermophilus HB8 genome and encodes a 131-amino-acid protein. The crystal structure of TTHA1544 has been determined at 2.0 A resolution by the single-wavelength anomalous dispersion method in order to elucidate its function. There are two molecules in the asymmetric unit. Each molecule consists of four alpha-helices and six beta-strands, with the beta-strands composing a central beta-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the alpha/beta-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized alpha/beta-hydrolase fold and that an additional component would be required for its activity. | ||
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- | Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8.,Xie Y, Takemoto C, Kishishita S, Uchikubo-Kamo T, Murayama K, Chen L, Liu ZJ, Wang BC, Manzoku M, Ebihara A, Kuramitsu S, Shirouzu M, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt, 12):993-7. Epub 2007 Nov 30. PMID:18084077<ref>PMID:18084077</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2dst" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Crystal Structure Analysis of TT1977
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Categories: Large Structures | Thermus thermophilus | Chen L | Kishishita S | Liu ZJ | Murayama K | Shirouzu M | Wang BC | Xie Y