2DST

Crystal Structure Analysis of TT1977

Summary for 2DST

• Entry DOI: 10.2210/pdb2dst/pdb
• Related: 2cyd
• Descriptor: Hypothetical protein TTHA1544 (2 entities in total)
• Functional Keywords: conserved hypothetical protein, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 28164.61

Authors

Xie, Y.,Kishishita, S.,Murayama, K.,Shirouzu, M.,Chen, L.,Liu, Z.J.,Wang, B.C.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-07-06, release date: 2007-01-06, Last modification date: 2024-03-13)

Primary citation

Xie, Y.,Takemoto, C.,Kishishita, S.,Uchikubo-Kamo, T.,Murayama, K.,Chen, L.,Liu, Z.J.,Wang, B.C.,Manzoku, M.,Ebihara, A.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8.
Acta Crystallogr.,Sect.F, 63:993-997, 2007

PubMed Abstract: 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.

PubMed: 18084077
DOI: 10.1107/S1744309107061106

Experimental method

X-RAY DIFFRACTION (2 Å)