caa a22 4500 397557752 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199605 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021320 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021320 Crystal Structure of Serratia Protease, a Zinc-Dependent Proteinase from Serratia sp. E-15, Containing a β-Sheet Coil Motif at 2.0AÅ Resolution [Elektronische Daten] [Kensaku Hamada, Yasuo Hata, Yoshio Katsuya, Hajime Hiramatsu, Takaji Fujiwara, Yukiteru Katsube] The crystal structure of Serratia protease from Serratia sp. E-15 was solved by the single isomorphous replacement method supplemented with anomalous scattering effects from both the Zn atom in the native crystal and the Sm atom in the derivative crystal, and refined at 2.0AÅ resolution to a crystallographic R-factor of 0.194. The enzyme consists of N-terminal catalytic and C-terminal β-sandwich domains, as observed in alkaline protease from Pseudomonas aeruginosa IFO3080. The catalytic domain with a five-stranded antiparallel β-sheet and five α-helices shares a basically common folding topology with those of other zinc metalloendoproteases. The catalytic zinc ion at the bottom of the active site cleft is ligated by Hisl76, Hisl80, His186, Tyr216, and a water molecule in a distorted trigonal-bipyramidal manner. The C-terminal domain is a β-strand-rich domain containing eighteen β-strands and a short α-helix, and has seven Ca2+ions bound to calcium binding loops. An unusual β-sheet coil motif is observed in this domain, where the β-strands and calcium binding loops are alternately incorporated into an elliptical right-handed spiral so as to form a two-layer untwisted β-sandwich structure. The Ca2+ ions in the C-terminal domain seem to be very important for the folding and stability of the β-sheet coil structure. © by the Journal of Biochemistry Regular Papers nationallicence β-sheet coil nationallicence crystal structure nationallicence metalloprotease nationallicence Serratia protease nationallicence Serratia sp. E-15 nationallicence Hamada Kensaku Faculty of Science, Shimane University Matsue,Shimane 690 aut Hata Yasuo Institute for Chemical Research, Kyoto University Uji, Kyoto 611 aut Katsuya Yoshio Hyogo Prefectural Institute of Industrial Technology Kobe, Hyogo 654 aut Hiramatsu Hajime Faculty of Science, Shimane University Matsue,Shimane 690 aut Fujiwara Takaji Faculty of Science, Shimane University Matsue,Shimane 690 aut Katsube Yukiteru Institute for Protein Research, Osaka University Suita, Osaka 565 aut The Journal of Biochemistry Oxford University Press 119/5(1996-05), 844-851 0021-924X 119:5<844 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021320 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021320 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hamada Kensaku Faculty of Science, Shimane University Matsue,Shimane 690 aut NATIONALLICENCE 700 1- Hata Yasuo Institute for Chemical Research, Kyoto University Uji, Kyoto 611 aut NATIONALLICENCE 700 1- Katsuya Yoshio Hyogo Prefectural Institute of Industrial Technology Kobe, Hyogo 654 aut NATIONALLICENCE 700 1- Hiramatsu Hajime Faculty of Science, Shimane University Matsue,Shimane 690 aut NATIONALLICENCE 700 1- Fujiwara Takaji Faculty of Science, Shimane University Matsue,Shimane 690 aut NATIONALLICENCE 700 1- Katsube Yukiteru Institute for Protein Research, Osaka University Suita, Osaka 565 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/5(1996-05), 844-851 0021-924X 119:5<844 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford