메뉴 건너뛰기




Volumn 47, Issue 13, 2008, Pages 4017-4027

Crystal structure of CYP105A1 (P450SU-1) in complex with 1α,25-dihydroxyvitamin D3

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIAN ENZYMES; SUBSTRATE-BINDING MECHANISM;

EID: 41449090375     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7023767     Document Type: Article
Times cited : (78)

References (52)
  • 1
    • 0001045385 scopus 로고
    • A new cytochrome in liver microsomes
    • Omura, T., and Sato, R. (1962) A new cytochrome in liver microsomes. J. Biol. Chem. 237, 1375-1376.
    • (1962) J. Biol. Chem , vol.237 , pp. 1375-1376
    • Omura, T.1    Sato, R.2
  • 3
    • 0033650404 scopus 로고    scopus 로고
    • The natural functions of secondary metabolites
    • Demain, A. L., and Fang, A. (2000) The natural functions of secondary metabolites. Adv. Biochem. Eng. Biotechnol. 69, 1-39.
    • (2000) Adv. Biochem. Eng. Biotechnol , vol.69 , pp. 1-39
    • Demain, A.L.1    Fang, A.2
  • 6
    • 0031755168 scopus 로고    scopus 로고
    • Current understanding of the molecular actions of vitamin D
    • Jones, G., Strugnell, S. A., and DeLuca, H. F. (1998) Current understanding of the molecular actions of vitamin D. Physiol. Rev. 78, 1193-1231.
    • (1998) Physiol. Rev , vol.78 , pp. 1193-1231
    • Jones, G.1    Strugnell, S.A.2    DeLuca, H.F.3
  • 10
    • 0015240863 scopus 로고
    • Identification of 1,25-dihydroxycholecalciferol, a new kidney hormone controlling calcium metabolism
    • Lawson, D. E., Fraser, D. R., Kodicek, E., Morris, H. R., and Williams, D. H. (1971) Identification of 1,25-dihydroxycholecalciferol, a new kidney hormone controlling calcium metabolism. Nature 230, 228-230.
    • (1971) Nature , vol.230 , pp. 228-230
    • Lawson, D.E.1    Fraser, D.R.2    Kodicek, E.3    Morris, H.R.4    Williams, D.H.5
  • 12
    • 0036806162 scopus 로고    scopus 로고
    • The human steroid hydroxylases CYP1B1 and CYP11B2
    • Bureik, M., Lisurek, M., and Bernhardt, R. (2002) The human steroid hydroxylases CYP1B1 and CYP11B2. Biol. Chem. 383, 1537-1551.
    • (2002) Biol. Chem , vol.383 , pp. 1537-1551
    • Bureik, M.1    Lisurek, M.2    Bernhardt, R.3
  • 14
    • 0037068964 scopus 로고    scopus 로고
    • Clinical importance of the cytochromes P450
    • Nebert, D. W., and Russell, D. W. (2002) Clinical importance of the cytochromes P450. Lancet 360, 1155-1162.
    • (2002) Lancet , vol.360 , pp. 1155-1162
    • Nebert, D.W.1    Russell, D.W.2
  • 15
    • 33646167609 scopus 로고    scopus 로고
    • Structural motif-based homology modeling of CYP27A1 and site-directed mutational analyses affecting vitamin D hydroxylation
    • Prosser, D. E., Guo, Y., Jia, Z., and Jones, G. (2006) Structural motif-based homology modeling of CYP27A1 and site-directed mutational analyses affecting vitamin D hydroxylation. Biophys. J. 90, 3389-3409.
    • (2006) Biophys. J , vol.90 , pp. 3389-3409
    • Prosser, D.E.1    Guo, Y.2    Jia, Z.3    Jones, G.4
  • 16
    • 3042601070 scopus 로고    scopus 로고
    • Homology modeling of human 25-hydroxyvitamin D3 1α-hydroxylase (CYP27B1) based on the crystal structure of rabbit CYP2C5
    • Yamamoto, K., Masuno, H., Sawada, N., Sakaki, T., Inouye, K., Ishiguro, M., and Yamada, S. (2004) Homology modeling of human 25-hydroxyvitamin D3 1α-hydroxylase (CYP27B1) based on the crystal structure of rabbit CYP2C5. J. Steroid Biochem. Mol. Biol. 89-90, 167-171.
    • (2004) J. Steroid Biochem. Mol. Biol , vol.89-90 , pp. 167-171
    • Yamamoto, K.1    Masuno, H.2    Sawada, N.3    Sakaki, T.4    Inouye, K.5    Ishiguro, M.6    Yamada, S.7
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W. A. (1991) Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 20
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E., and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • de La Fortelle, E.1    Bricogne, G.2
  • 22
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R. J., Perrakis, A., and Lamzin, V. S. (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374, 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., Sect. A: Found. Crystallogr. 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: Programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: Programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
  • 26
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 27
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G. J., and Jones, T. A. (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 178-185.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 28
    • 0022273620 scopus 로고
    • The 2.6-Å crystal structure of Pseudomonas putida cytochrome P-450
    • Poulos, T. L., Finzel, B. C., Gunsalus, I. C., Wagner, G. C., and Kraut, J. (1985) The 2.6-Å crystal structure of Pseudomonas putida cytochrome P-450. J. Biol. Chem. 260, 16122-16130.
    • (1985) J. Biol. Chem , vol.260 , pp. 16122-16130
    • Poulos, T.L.1    Finzel, B.C.2    Gunsalus, I.C.3    Wagner, G.C.4    Kraut, J.5
  • 29
    • 0027994378 scopus 로고
    • A role for Asp-251 in cytochrome P-450cam oxygen activation
    • Gerber, N. C., and Sligar, S. G. (1994) A role for Asp-251 in cytochrome P-450cam oxygen activation. J. Biol. Chem. 269, 4260-4266.
    • (1994) J. Biol. Chem , vol.269 , pp. 4260-4266
    • Gerber, N.C.1    Sligar, S.G.2
  • 30
    • 0001541099 scopus 로고
    • Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: Possible role of the hydroxy amino acid in oxygen activation
    • Imai, M., Shimada, H., Watanabe, Y., Matsushima-Hibiya, Y., Makino, R., Koga, H., Horiuchi, T., and Ishimura, Y. (1989) Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: Possible role of the hydroxy amino acid in oxygen activation. Proc. Natl. Acad. Sci. U.S.A. 86, 7823-7827.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 7823-7827
    • Imai, M.1    Shimada, H.2    Watanabe, Y.3    Matsushima-Hibiya, Y.4    Makino, R.5    Koga, H.6    Horiuchi, T.7    Ishimura, Y.8
  • 36
    • 0037809271 scopus 로고    scopus 로고
    • The 1.92-Å structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems
    • Podust, L. M., Kim, Y., Arase, M., Neely, B. A., Beck, B. J., Bach, H., Sherman, D. H., Lamb, D. C., Kelly, S. L., and Waterman, M. R. (2003) The 1.92-Å structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems. J. Biol. Chem. 278, 12214-12221.
    • (2003) J. Biol. Chem , vol.278 , pp. 12214-12221
    • Podust, L.M.1    Kim, Y.2    Arase, M.3    Neely, B.A.4    Beck, B.J.5    Bach, H.6    Sherman, D.H.7    Lamb, D.C.8    Kelly, S.L.9    Waterman, M.R.10
  • 37
    • 0242582120 scopus 로고    scopus 로고
    • Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK
    • Nagano, S., Li, H., Shimizu, H., Nishida, C., Ogura, H., Ortiz de Montellano, P. R., and Poulos, T. L. (2003) Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK. J. Biol. Chem. 278, 44886-44893.
    • (2003) J. Biol. Chem , vol.278 , pp. 44886-44893
    • Nagano, S.1    Li, H.2    Shimizu, H.3    Nishida, C.4    Ogura, H.5    Ortiz de Montellano, P.R.6    Poulos, T.L.7
  • 38
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li, H., and Poulos, T. L. (1997) The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat. Struct. Biol. 4, 140-146.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 39
    • 0037646516 scopus 로고    scopus 로고
    • Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies
    • Lee, D. S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S. Y., and Shiro, Y. (2003) Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies. J. Biol. Chem. 278, 9761-9767.
    • (2003) J. Biol. Chem , vol.278 , pp. 9761-9767
    • Lee, D.S.1    Yamada, A.2    Sugimoto, H.3    Matsunaga, I.4    Ogura, H.5    Ichihara, K.6    Adachi, S.7    Park, S.Y.8    Shiro, Y.9
  • 41
    • 0037117562 scopus 로고    scopus 로고
    • Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine
    • Winn, P. J., Ludemann, S. K., Gauges, R., Lounnas, V., and Wade, R. C. (2002) Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine. Proc. Natl. Acad. Sci. U.S.A. 99, 5361-5366.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 5361-5366
    • Winn, P.J.1    Ludemann, S.K.2    Gauges, R.3    Lounnas, V.4    Wade, R.C.5
  • 42
    • 0141925683 scopus 로고    scopus 로고
    • NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes
    • Tosha, T., Yoshioka, S., Takahashi, S., Ishimori, K., Shimada, H., and Morishima, I. (2003) NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes. J. Biol. Chem. 278, 39809-39821.
    • (2003) J. Biol. Chem , vol.278 , pp. 39809-39821
    • Tosha, T.1    Yoshioka, S.2    Takahashi, S.3    Ishimori, K.4    Shimada, H.5    Morishima, I.6
  • 43
    • 0024442346 scopus 로고
    • Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase
    • Matsuoka, T., Miyakoshi, S., Tanzawa, K., Nakahara, K., Hosobuchi, M., and Serizawa, N. (1989) Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase. Eur. J. Biochem. 184, 707-713.
    • (1989) Eur. J. Biochem , vol.184 , pp. 707-713
    • Matsuoka, T.1    Miyakoshi, S.2    Tanzawa, K.3    Nakahara, K.4    Hosobuchi, M.5    Serizawa, N.6
  • 44
    • 0033527407 scopus 로고    scopus 로고
    • Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: Heterologous expression, activity, and activation effects of multiple xenobiotics
    • Taylor, M., Lamb, D. C., Cannell, R., Dawson, M., and Kelly, S. L. (1999) Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: Heterologous expression, activity, and activation effects of multiple xenobiotics. Biochem. Biophys. Res. Commun. 263, 838-842.
    • (1999) Biochem. Biophys. Res. Commun , vol.263 , pp. 838-842
    • Taylor, M.1    Lamb, D.C.2    Cannell, R.3    Dawson, M.4    Kelly, S.L.5
  • 46
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T. L., Finzel, B. C., and Howard, A. J. (1987) High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195, 687-700.
    • (1987) J. Mol. Biol , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 47
    • 0029116115 scopus 로고
    • NMR studies of substrate binding to cytochrome P450 BM3: Comparisons to cytochrome P450 cam
    • Modi, S., Primrose, W. U., Boyle, J. M., Gibson, C. F., Lian, L. Y., and Roberts, G. C. (1995) NMR studies of substrate binding to cytochrome P450 BM3: Comparisons to cytochrome P450 cam. Biochemistry 34, 8982-8988.
    • (1995) Biochemistry , vol.34 , pp. 8982-8988
    • Modi, S.1    Primrose, W.U.2    Boyle, J.M.3    Gibson, C.F.4    Lian, L.Y.5    Roberts, G.C.6
  • 48
    • 0029876059 scopus 로고    scopus 로고
    • The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction
    • Modi, S., Sutcliffe, M. J., Primrose, W. U., Lian, L. Y., and Roberts, G. C. (1996) The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction. Nat. Struct. Biol. 3, 414-417.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 414-417
    • Modi, S.1    Sutcliffe, M.J.2    Primrose, W.U.3    Lian, L.Y.4    Roberts, G.C.5
  • 49
    • 33748750539 scopus 로고    scopus 로고
    • The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • Sherman, D. H., Li, S., Yermalitskaya, L. V., Kim, Y., Smith, J. A., Waterman, M. R., and Podust, L. M. (2006) The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J. Biol. Chem. 281, 26289-26297.
    • (2006) J. Biol. Chem , vol.281 , pp. 26289-26297
    • Sherman, D.H.1    Li, S.2    Yermalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6    Podust, L.M.7
  • 50
    • 0026319298 scopus 로고
    • Biosynthesis and intracellular sorting of mitochondrial forms of cytochrome P450
    • Omura, T., and Ito, A. (1991) Biosynthesis and intracellular sorting of mitochondrial forms of cytochrome P450. Methods Enzymol. 206, 75-81.
    • (1991) Methods Enzymol , vol.206 , pp. 75-81
    • Omura, T.1    Ito, A.2
  • 51
    • 0028109245 scopus 로고
    • Alterations of the regiospecificity of progesterone metabolism by the mutagenesis of two key amino acid residues in rabbit cytochrome P450 2C3v
    • Richardson, T. H., and Johnson, E. F. (1994) Alterations of the regiospecificity of progesterone metabolism by the mutagenesis of two key amino acid residues in rabbit cytochrome P450 2C3v. J. Biol. Chem. 269, 23937-23943.
    • (1994) J. Biol. Chem , vol.269 , pp. 23937-23943
    • Richardson, T.H.1    Johnson, E.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.