1WJ9

Crystal structure of a CRISPR-associated protein from thermus thermophilus

Summary for 1WJ9

• Entry DOI: 10.2210/pdb1wj9/pdb
• Descriptor: CRISPR-associated protein (2 entities in total)
• Functional Keywords: alpha and beta protein, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 23763.69

Authors

Ebihara, A.,Yao, M.,Yokoyama, S.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-29, release date: 2004-11-29, Last modification date: 2024-03-13)

Primary citation

Ebihara, A.,Yao, M.,Masui, R.,Tanaka, I.,Yokoyama, S.,Kuramitsu, S.
Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif-like domain
Protein Sci., 15:1494-1499, 2006

PubMed Abstract: We have determined the crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 at 1.9 A resolution. This protein is a member of the Escherichia coli ygcH sequence family, which contains approximately 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 beta-sheet packed on one side by alpha-helices. These two tandem domains face each other to generate a beta-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 beta-sheet platform formed by two tandem repeats of an RNA recognition motif domain with signature sequence motifs on the beta-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 beta-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.

PubMed: 16672237
DOI: 10.1110/ps.062131106

Experimental method

X-RAY DIFFRACTION (1.9 Å)