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Volumn 389, Issue 2, 2009, Pages 310-314

Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli

Author keywords

Calcium binding; Cleavage; Escherichia coli; HycI; Hydrogenase; Maturation; Metal ion; Protease; X ray; X ray crystallography

Indexed keywords

CALCIUM ION; ENDOPEPTIDASE HYCI; HYDROGENASE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 70349332445     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.135     Document Type: Article
Times cited : (15)

References (36)
  • 2
    • 0031574022 scopus 로고    scopus 로고
    • Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
    • Higuchi Y., Yagi T., and Yasuoka N. Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure 5 (1997) 1671-1680
    • (1997) Structure , vol.5 , pp. 1671-1680
    • Higuchi, Y.1    Yagi, T.2    Yasuoka, N.3
  • 6
    • 0029757989 scopus 로고    scopus 로고
    • Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form
    • Maier T., and Böck A. Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form. Biochemistry 35 (1996) 10089-10093
    • (1996) Biochemistry , vol.35 , pp. 10089-10093
    • Maier, T.1    Böck, A.2
  • 8
    • 0033591263 scopus 로고    scopus 로고
    • Crystal structure of the hydrogenase maturating endopeptidase HYPD from Escherichia coli
    • Fritsche E., Paschos A., Beisel H.G., Böck A., and Huber R. Crystal structure of the hydrogenase maturating endopeptidase HYPD from Escherichia coli. J. Mol. Biol. 288 (1999) 989-998
    • (1999) J. Mol. Biol. , vol.288 , pp. 989-998
    • Fritsche, E.1    Paschos, A.2    Beisel, H.G.3    Böck, A.4    Huber, R.5
  • 9
    • 0028832110 scopus 로고
    • Characterisation of a protease from Escherichia coli involved in hydrogenase maturation
    • Rossmann R., Maier T., Lottspeich F., and Böck A. Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. Eur. J. Biochem. 227 (1995) 545-550
    • (1995) Eur. J. Biochem. , vol.227 , pp. 545-550
    • Rossmann, R.1    Maier, T.2    Lottspeich, F.3    Böck, A.4
  • 10
    • 0025975104 scopus 로고
    • Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli
    • Lutz S., Jacobi A., Schlensog V., Bohm R., Sawers G., and Bock A. Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5 (1991) 123-135
    • (1991) Mol. Microbiol. , vol.5 , pp. 123-135
    • Lutz, S.1    Jacobi, A.2    Schlensog, V.3    Bohm, R.4    Sawers, G.5    Bock, A.6
  • 11
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • Olson J.W., Mehta N.S., and Maier R.J. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol. Microbiol. 39 (2001) 176-182
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 12
    • 0022632813 scopus 로고
    • Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity
    • Waugh R., and Boxer D.H. Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity. Biochimie 68 (1986) 157-166
    • (1986) Biochimie , vol.68 , pp. 157-166
    • Waugh, R.1    Boxer, D.H.2
  • 13
    • 0027450599 scopus 로고
    • The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein
    • Maier T., Jacobi A., Sauter M., and Böck A. The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein. J. Bacteriol. 175 (1993) 630-635
    • (1993) J. Bacteriol. , vol.175 , pp. 630-635
    • Maier, T.1    Jacobi, A.2    Sauter, M.3    Böck, A.4
  • 14
    • 0345647107 scopus 로고    scopus 로고
    • Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation
    • Drapal N., and Böck A. Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation. Biochemistry 37 (1998) 2941-2948
    • (1998) Biochemistry , vol.37 , pp. 2941-2948
    • Drapal, N.1    Böck, A.2
  • 15
    • 0040355752 scopus 로고    scopus 로고
    • Analysis of the HypC-HycE complex, a key intermediate in the assembly of the metal center of the Escherichia coli hydrogenase 3
    • Magalon A., and Böck A. Analysis of the HypC-HycE complex, a key intermediate in the assembly of the metal center of the Escherichia coli hydrogenase 3. J. Biol. Chem. 275 (2000) 21114-21120
    • (2000) J. Biol. Chem. , vol.275 , pp. 21114-21120
    • Magalon, A.1    Böck, A.2
  • 16
    • 17644429864 scopus 로고    scopus 로고
    • Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation
    • Magalon A., and Böck A. Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation. FEBS Lett. 473 (2000) 254-258
    • (2000) FEBS Lett. , vol.473 , pp. 254-258
    • Magalon, A.1    Böck, A.2
  • 17
    • 7044222771 scopus 로고    scopus 로고
    • The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases
    • Blokesch M., Albracht S.P.J., Matzanke B.F., Drapal N.M., Jacobi A., and Böck A. The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J. Mol. Biol. 344 (2004) 155-167
    • (2004) J. Mol. Biol. , vol.344 , pp. 155-167
    • Blokesch, M.1    Albracht, S.P.J.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Böck, A.6
  • 18
    • 33745867578 scopus 로고    scopus 로고
    • Properties of the [NiFe]-hydrogenase maturation protein HypD
    • Blokesch M., and Böck A. Properties of the [NiFe]-hydrogenase maturation protein HypD. FEBS Lett. 580 (2006) 4065-4068
    • (2006) FEBS Lett. , vol.580 , pp. 4065-4068
    • Blokesch, M.1    Böck, A.2
  • 19
    • 0036440688 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle
    • Blokesch M., and Böck A. Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle. J. Mol. Biol. 324 (2002) 287-296
    • (2002) J. Mol. Biol. , vol.324 , pp. 287-296
    • Blokesch, M.1    Böck, A.2
  • 20
    • 4344582395 scopus 로고    scopus 로고
    • Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE
    • Blokesch M., Paschos A., Bauer A., Reissmann S., Drapal N., and Böck A. Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur. J. Biochem. 271 (2004) 3428-3436
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3428-3436
    • Blokesch, M.1    Paschos, A.2    Bauer, A.3    Reissmann, S.4    Drapal, N.5    Böck, A.6
  • 22
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
    • Rossmann R., Sauter M., Lottspeich F., and Bock A. Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537. Eur. J. Biochem. 220 (1994) 377-384
    • (1994) Eur. J. Biochem. , vol.220 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Bock, A.4
  • 23
    • 0026714545 scopus 로고
    • Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii
    • Gollin D.J., Mortenson L.E., and Robson R.L. Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii. FEBS Lett. 309 (1992) 371-375
    • (1992) FEBS Lett. , vol.309 , pp. 371-375
    • Gollin, D.J.1    Mortenson, L.E.2    Robson, R.L.3
  • 24
    • 0034031960 scopus 로고    scopus 로고
    • Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation
    • Theodoratou E., Paschos A., Magalon A., Fritsche E., Huber R., and Bock A. Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation. Eur. J. Biochem. 267 (2000) 1995-1999
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1995-1999
    • Theodoratou, E.1    Paschos, A.2    Magalon, A.3    Fritsche, E.4    Huber, R.5    Bock, A.6
  • 25
    • 0028157325 scopus 로고
    • In vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase in Azotobacter vinelandii
    • Menon A.L., and Ronson R.L. In vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase in Azotobacter vinelandii. J. Bacteriol. 176 (1994) 291-295
    • (1994) J. Bacteriol. , vol.176 , pp. 291-295
    • Menon, A.L.1    Ronson, R.L.2
  • 26
    • 34250874525 scopus 로고    scopus 로고
    • Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling
    • Watanabe S., Matsumi R., Arai T., Atomi H., Imanaka T., and Miki K. Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling. Mol. Cell 27 (2007) 29-40
    • (2007) Mol. Cell , vol.27 , pp. 29-40
    • Watanabe, S.1    Matsumi, R.2    Arai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 27
    • 33947536028 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation
    • Yang F., Hu W., Xu H., Li C., Xia B., and Jin C. Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation. J. Biol. Chem. 282 (2007) 3856-3863
    • (2007) J. Biol. Chem. , vol.282 , pp. 3856-3863
    • Yang, F.1    Hu, W.2    Xu, H.3    Li, C.4    Xia, B.5    Jin, C.6
  • 28
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson A. Current approaches to macromolecular crystallization. Eur. J. Biochem. 189 (1990) 1-23
    • (1990) Eur. J. Biochem. , vol.189 , pp. 1-23
    • McPherson, A.1
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
  • 31
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 35
    • 0036922194 scopus 로고    scopus 로고
    • Observation of additional calcium ion in the crystal structure of the triple mutant K56, 120, 121M of bovine pancreatic phospholipase A2
    • Rajakannan V., Yogavel M., Poi M.J., Jeyaprakash A., Jeyakanthan J., Velmurugan D., Tsai M.D., and Sekar K. Observation of additional calcium ion in the crystal structure of the triple mutant K56, 120, 121M of bovine pancreatic phospholipase A2. J. Mol. Biol. 324 (2002) 755-762
    • (2002) J. Mol. Biol. , vol.324 , pp. 755-762
    • Rajakannan, V.1    Yogavel, M.2    Poi, M.J.3    Jeyaprakash, A.4    Jeyakanthan, J.5    Velmurugan, D.6    Tsai, M.D.7    Sekar, K.8
  • 36
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., and Sander C. Mapping the protein universe. Science 273 (1996) 595-603
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2


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