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PROTEIN STRUCTURE REPORT

Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif-like domain

¹ RIKEN SPring-8 Center, Harima Institute, Hyogo 679-5148, Japan
² Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan
³ Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
⁴ Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
⁵ RIKEN Genomic Sciences Center, Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan

(RECEIVED February 2, 2006; FINAL REVISION February 2, 2006; ACCEPTED February 21, 2006)

We have determined the crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 at 1.9 Å resolution. This protein is a member of the Escherichia coli ygcH sequence family, which contains 15 sequence homologs of bacterial origin. These homologs have a high isoelectric point. The crystal structure reveals that TTHB192 consists of two independently folded domains, and that each domain exhibits a ferredoxin-like fold with a four-stranded antiparallel -sheet packed on one side by -helices. These two tandem domains face each other to generate a -sheet platform. TTHB192 displays overall structural similarity to Sex-lethal protein and poly(A)-binding protein fragments. These proteins have RNA binding activity which is supported by a -sheet platform formed by two tandem repeats of an RNA recognition motif domain with signature sequence motifs on the -sheet surface. Although TTHB192 does not have the same signature sequence motif as the RNA recognition motif domain, the presence of an evolutionarily conserved basic patch on the -sheet platform could be functionally relevant for nucleic acid-binding. This report shows that TTHB192 and its sequence homologs adopt an RNA recognition motif-like domain and provides the first testable functional hypothesis for this protein family.

Keywords: structural genomics; hypothetical protein; ygcH; ferredoxin-like fold; RNA recognition motif

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