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Published online before print April 5, 2006, 10.1110/ps.062148506
Protein Science (2006), 15:1187-1192. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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PROTEIN STRUCTURE REPORT

Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 Å resolution: A CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD

Kaori Ito1,5, Ryoichi Arai1,2,5, Emiko Fusatomi1, Tomomi Kamo-Uchikubo1, Shin-ichi Kawaguchi2, Ryogo Akasaka1, Takaho Terada1,2, Seiki Kuramitsu2,3, Mikako Shirouzu1,2 and Shigeyuki Yokoyama1,2,4

1 Protein Research Group, RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan
2 RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148, Japan
3 Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
4 Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan

(RECEIVED February 10, 2006; FINAL REVISION February 10, 2006; ACCEPTED February 16, 2006)

TTHA0727 is a conserved hypothetical protein from Thermus thermophilus HB8, with a molecular mass of 12.6 kDa. TTHA0727 belongs to the carboxymuconolactone decarboxylase (CMD) family (Pfam 02627). A sequence comparison with its homologs suggested that TTHA0727 is a distinct protein from alkylhydroperoxidase AhpD and {gamma}-carboxymuconolactone decarboxylase in the CMD family. Here we report the 1.9 Å crystal structure of TTHA0727 (PDB ID: 2CWQ) determined by the multiwavelength anomalous dispersion method. The TTHA0727 monomer structure consists of seven {alpha}-helices ({alpha}1–{alpha}7) and one short 310-helix. The crystal structure and the analytical ultracentrifugation revealed that TTHA0727 forms a hexameric ring structure in solution. The electrostatic potential distribution on the solvent-accessible surface of the TTHA0727 hexamer showed that positively charged regions exist on the side of the ring structure, suggesting that TTHA0727 interacts with some negatively charged molecules. A structural homology search revealed that the structure of three {alpha}-helices ({alpha}4–{alpha}6) is remarkably conserved, suggesting that it is the common structural motif for the CMD family proteins. In addition, the nine residues of the N-terminal tag bound to the cleft region between {alpha}1 and {alpha}3 in chains A and B of TTHA0727, implying that this region is the putative binding/active site for some small molecules.

Keywords: extremely thermophilic bacteria; Thermus thermophilus HB8; hypothetical protein; TTHA0727 (TT1628); carboxymuconolactone decarboxylase (CMD) family; hexameric ring structure; structural genomics/proteomics


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Copyright © 2006 by The Protein Society.