Structure of an integral membrane sterol reductase from Methylomicrobium alcaliphilum

Nature

Volumn 517, Issue 7532, 2015, Pages 104-107

  Li, Xiaochun ^a   Roberti, Rita ^b   Blobel, Gunter ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF PERUGIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID 5BETA REDUCTASE; STEROL; 7-DEHYDROCHOLESTEROL REDUCTASE; CELL RECEPTOR; CHOLESTEROL; DELTA(14)-STEROL REDUCTASE; LAMIN B RECEPTOR; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TM7SF2 PROTEIN, HUMAN;

BACTERIUM; CHEMICAL BONDING; CYTOPLASM; ENZYME ACTIVITY; LIPID; MEMBRANE; MUTATION; PUBLIC HEALTH; STEROL;

ARTICLE; CHOLESTEROL SYNTHESIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HEK293 CELL LINE; HUMAN; HUMAN CELL; HYDROGEN BOND; LIPID BILAYER; METHANOTROPHIC BACTERIUM; METHYLOMICROBIUM ALCALIPHILUM; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; BINDING SITE; BIOSYNTHESIS; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; METHYLOCOCCACEAE; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); METHYLOBACTER ALCALIPHILUS;

BINDING SITES; CATALYTIC DOMAIN; CELL MEMBRANE; CHOLESTEROL; CRYSTALLOGRAPHY, X-RAY; HUMANS; MEMBRANE PROTEINS; METHYLOCOCCACEAE; MODELS, MOLECULAR; NADP; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; STEROLS;

EID: 84923196528     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13797     Document Type: Article

References (36)

1. Porter, F. D. & Herman, G. E. Malformation syndromes caused by disorders of cholesterol synthesis. J. Lipid Res. 52, 6-34 (2011).
2. Worman, H. J., Yuan, J., Blobel, G. & Georgatos, S. D. A lamin B receptor in the nuclear envelope. Proc. Natl Acad. Sci. USA 85, 8531-8534 (1988).
3. Di Costanzo, L., Drury, J. E., Penning, T. M.& Christianson, D. W. Crystal structure of human liver D4-3-ketosteroid 5b-reductase (AKR1D1) and implications for substrate binding and catalysis. J. Biol. Chem. 283, 16830-16839 (2008).
4. Fahy, E. et al. A comprehensive classification system for lipids. J. Lipid Res. 46, 839-862 (2005).
5. Miller, W. L. & Bose, H. S. Early steps in steroidogenesis: intracellular cholesterol trafficking. J. Lipid Res. 52, 2111-2135 (2011).
6. Miller, W. L. Steroid hormone synthesis in mitochondria. Mol. Cell. Endocrinol. 379, 62-73 (2013).
7. Goldstein, J. L., DeBose-Boyd, R. A. & Brown, M. S. Protein sensors for membrane sterols. Cell 124, 35-46 (2006).
8. Olins, A. L., Rhodes, G., Welch, D. B., Zwerger, M. & Olins, D. E. Lamin B receptor: multi-tasking at the nuclear envelope. Nucleus 1, 53-70 (2010).
9. Silve, S., Dupuy, P. H., Ferrara, P. & Loison, G. Human lamin B receptor exhibits sterol C14-reductase activity in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1392, 233-244 (1998).
10. Hoffmann, K. et al. Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huët anomaly). Nature Genet. 31, 410-414 (2002).
11. Waterham, H. R. et al. Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3b-hydroxysterol D14-reductase deficiency due to mutations in the lamin B receptor gene. Am. J. Hum. Genet. 72, 1013-1017 (2003).
12. Porter, F. D. Smith-Lemli-Opitz syndrome: pathogenesis, diagnosis and management. Eur. J. Hum. Genet. 16, 535-541 (2008).
13. Herman, G. E. & Kratz, L. Disorders of sterol synthesis: beyond Smith-Lemli-Opitz syndrome. Am. J. Med. Genet. C 160, 301-321 (2012).
14. Shchukin, V. N., Khmelenina, V. N., Eshinimaev, B., Suzina, N. E. & Trotsenko, Y. A. Primary characterization of dominant cell surface proteins of halotolerant methanotroph Methylomicrobium alcaliphilum 20Z. Microbiology 80, 595-605 (2011).
15. Paik, Y. K., Trzaskos, J. M., Shafiee, A. & Gaylor, J. L. Microsomal enzymes of cholesterol biosynthesis from lanosterol. Characterization, solubilization, and partialpurification ofNADPH-dependentD8,14-steroid 14-reductase. J. Biol. Chem. 259, 13413-13423 (1984).
16. Roberti, R. et al. Cloning and expression of sterol D14-reductase from bovine liver. Eur. J. Biochem. 269, 283-290 (2002).
17. Bennati, A. M. et al. Sterol dependent regulation of human TM7SF2 gene expression: role of the encoded 3b-hydroxysterol D14-reductase in human cholesterol biosynthesis. Biochim. Biophys. Acta 1761, 677-685 (2006).
18. von Heijne, G. Control of topology andmode of assembly of a polytopicmembrane protein by positively charged residues. Nature 341, 456-458 (1989).
19. Kim, H., Melen, K., Osterberg, M. & von Heijne, G. A global topology map of the Saccharomyces cerevisiae membrane proteome. Proc. Natl Acad. Sci. USA 103, 11142-11147 (2006).
20. Miller, W. L. & Auchus, R. J. The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders. Endocr. Rev. 32, 81-151 (2011).
21. Bennati, A. M. et al. Disruption of the gene encoding 3b-hydroxysterol D14-reductase (Tm7sf2) in mice does not impair cholesterol biosynthesis. FEBS J. 275, 5034-5047 (2008).
22. Yang, J. et al. Mechanism of isoprenylcysteine carboxyl methylation from the crystal structure of the integral membrane methyltransferase ICMT. Mol. Cell 44, 997-1004 (2011).
23. Hennekes, H. & Nigg, E. A. The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J. Cell Sci. 107, 1019-1029 (1994).
24. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
25. Zwart, P. H., Grosse-Kunstleve, R. W. & Adams, P. D. Xtriage and Fest: automatic assessment of X-ray data and substructure structure factor estimation. CCP4 Newsletter 43, 27 (2005).
26. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
27. Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861 (1999).
28. Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. Acta Crystallogr. D 58, 1772-1779 (2002).
29. McCoy, A. J. et al.Phaser crystallographic software. J.Appl. Crystallogr.40, 658-674 (2007).
30. Cowtan, K. dm: An automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallogr. 31, 34-38 (1994).
31. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
32. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
33. Fiser, A.& Sali, A.Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol. 374, 461-491 (2003).
34. Thompson, J. D., Higgins, D. G.&Gibson, T. J.CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (1994).
35. Clayton, P. et al. Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein. Nucleus 1, 354-366 (2010).
36. Holm, L. & Rosenstrom, P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).