Crystal structure of TTHA1264, a putative M16‐family zinc peptidase from Thermus thermophilus HB8 that is homologous to the β subunit of mitochondrial processing peptidase
Copyright policy )Crystal structure of TTHA1264, a putative M16‐family zinc peptidase from Thermus thermophilus HB8 that is homologous to the β subunit of mitochondrial processing peptidase
Crystal structure of TTHA1264, a putative M16-family zinc peptidase from Thermus thermophilus HB8 that is homologous to the b subunit of mitochondrial processing peptidase Jun Ohtsuka, Yosuke Ichihara, Akio Ebihara, Koji Nagata, and Masaru Tanokura* 1Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan 2 RIKEN SPring-8 Center, Harima Institute, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan
- University of Tokyo Japan
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Thermus thermophilus, Molecular Sequence Data, Metalloendopeptidases, Crystallography, X-Ray, Protein Structure, Secondary, Recombinant Proteins, Protein Structure, Tertiary, Mitochondrial Processing Peptidase, Zinc, Bacterial Proteins, Escherichia coli, Metalloproteases, Amino Acid Sequence, Protein Multimerization, Protein Structure, Quaternary, Protein Binding
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Thermus thermophilus, Molecular Sequence Data, Metalloendopeptidases, Crystallography, X-Ray, Protein Structure, Secondary, Recombinant Proteins, Protein Structure, Tertiary, Mitochondrial Processing Peptidase, Zinc, Bacterial Proteins, Escherichia coli, Metalloproteases, Amino Acid Sequence, Protein Multimerization, Protein Structure, Quaternary, Protein Binding
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