Crystal structure of human μ-crystallin complexed with NADPH

Protein Science

Volumn 16, Issue 2, 2007, Pages 329-335

  Cheng, Zhongjun ^a,b   Sun, Lihua ^c   He, Jianhua ^c   Gong, Weimin ^a,b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^c SHANGHAI INSTITUTE OF APPLIED PHYSICS   (China)

Author keywords

crystallin; cis trans isomerization of proline; Crystal structure; Nonsyndromic deafness; p38 cytosolic 3,5,3 triiodo L thyronine binding protein; T 3 binding site

Indexed keywords

ALANINE DEHYDROGENASE; ARGININE; CRYSTALLIN; DIMER; HISTONE; MONOMER; ORNITHINE; PROLINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; VALINE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; GENE OVEREXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY;

ALANINE DEHYDROGENASE; AMINO ACID SEQUENCE; AMMONIA-LYASES; ANIMALS; BINDING SITES; CATTLE; CRYSTALLINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STEREOISOMERISM;

ARCHAEOGLOBUS FULGIDUS; BACTERIA (MICROORGANISMS); PSEUDOMONAS PUTIDA;

EID: 33846515191     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062556907     Document Type: Article

References (33)

1. Abe, S., Katagiri, T., Saito-Hisaminato, A., Usami, S., Inoue, Y., Tsunoda, T., and Nakamura, Y. 2003. Identification of CRYM as a candidate responsible for nonsyndromic deafness, through cDNA microarray analysis of human cochlear and vestibular tissues. Am. J. Hum. Genet. 72: 73-82.
2. Beslin, A., Vie, M.P., Blondeau, J.P., and Francon, J. 1995. Identification by photoaffinity labelling of a pyridine nucleotide-dependent tri-iodothyronine-binding protein in the cytosol of cultured astroglial cells. Biochem. J. 305: 729-737.
3. Bottoms, C.A., Smith, P.E., and Tanner, J.J. 2002. A structurally conserved water molecule in Rossmann dinucleotide-binding domains. Protein Sci. 11: 2125-2137.
4. Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54: 905-921.
5. Carugo, O. and Argos, P. 1997. NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins 28: 10-28.
6. Chen, H., Phillips, H.A., Callen, D.F., Kim, R.Y., Wistow, G.J., and Antonarakis, S.E. 1992. Localization of the human gene for μ-crystallin to chromosome 16p. Genomics 14: 1115-1116.
7. DeLano, W.L. 2002. The PyMOL user's manual. DeLano Scientific, San Carlos, CA.
8. Emsley, P. and Cowtan, K. 2004. Coot: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60: 2126-2132.
9. Gallagher, D.T., Monbouquette, H.G., Schroder, I., Robinson, H., Holden, M.J., and Smith, N.N. 2004. Structure of alanine dehydrogenase from Archaeoglobus: Active site analysis and relation to bacterial cyclodeaminases and mammalian m crystallin. J. Mol. Biol. 342: 119-130.
10. Goodman, J.L., Wang, S., Alam, S., Ruzicka, F.J., Frey, P.A., and Wedekind, J.E. 2004. Ornithine cyclodeaminase: Structure, mechanism of action, and implications for the μ-crystallin family. Biochemistry 43: 13883-13891.
11. Gouet, P., Courcelle, E., Stuart, D.I., and Metoz, F. 1999. ESPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
12. Hashizume, K., Kobayashi, M., and Miyamoto, T. 1986. Active and inactive forms of 3,5,3′-triiodo-L-thyronine (T3)-binding protein in rat kidney cytosol: Possible role of nicotinamide adenine dinucleotide phosphate in activation of T3 binding. Endocrinology 119: 710-719.
13. Hashizume, K., Miyamoto, T., Ichikawa, K., Yamauchi, K., Sakurai, A., Ohtsuka, H., Kobayashi, M., Nishii, Y., and Yamada, T. 1989. Evidence for the presence of two active forms of cytosolic 3,5,3′-triiodo-L-thyronine (T3)-binding protein (CTBP) in rat kidney. Specialized functions of two CTBPs in intracellular T3 translocation. J. Biol. Chem. 264: 4864-4871.
14. Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
15. Kim, R.Y., Gasser, R., and Wistow, G.J. 1992. μ-Crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina. Proc. Natl. Acad. Sci. 89: 9292-9296.
16. Kohrle, J. 1999. Local activation and inactivation of thyroid hormones: The deiodinase family. Mol. Cell. Endocrinol. 151: 103-119.
17. Langsetmo, K., Fuchs, J., and Woodward, C. 1989. Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation. Biochemistry 28: 3211-3220.
18. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
19. 3-mediated transactivation. Endocrinology 143: 1538-1544.
20. Ondo-Mbele, E., Vives, C., Kone, A., and Serre, L. 2005. Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant. J. Mol. Biol. 347: 555-563.
21. Oshima, A., Suzuki, S., Takumi, Y., Hashizume, K., Abe, S., and Usami, S. 2006. CRYM mutations cause deafness through thyroid hormone binding properties in the fibrocytes of the cochlea. J. Med. Genet. 43: e25.
22. Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
23. Rossmann, M.G., Moras, D., and Olsen, K.W. 1974. Chemical and biological evolution of nucleotide-binding protein. Nature 250: 194-199.
24. Schroder, I., Vadas, A., Johnson, E., Lim, S., and Monbouquette, H.G. 2004. A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and μ-crystallin. J. Bacteriol. 186: 7680-7689.
25. Segovia, L., Horwitz, J., Gasser, R., and Wistow, G. 1997. Two roles for mcrystallin: A lens structural protein in diurnal marsupials and a possible enzyme in mammalian retinas. Mol. Vis. 3: 9.
26. Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. 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.
27. Truckses, D.M., Somoza, J.R., Prehoda, K.E., Miller, S.C., and Markley, J.L. 1996. Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease. Protein Sci. 5: 1907-1916.
28. Vagin, A. and Teplyakov, A. 1997. MOLREP: An automated program for molecular replacement. J. Appl. Crystallogr. 30: 1022-1025.
29. Vie, M.P., Evrard, C., Osty, J., Breton-Gilet, A., Blanchet, P., Pomerance, M., Rouget, P., Francon, J., and Blondeau, J.P. 1997. Purification, molecular cloning, and functional expression of the human nicodinamide-adenine dinucleotide phosphate-regulated thyroid hormone-binding protein. Mol. Endocrinol. 11: 1728-1736.
30. Wallace, A.C., Laskowski, R.A., and Thornton, J.M. 1995. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8: 127-134.
31. Wistow, G. and Kim, H. 1991. Lens protein expression in mammals: Taxon-specificity and the recruitment of crystallins. J. Mol. Evol. 32: 262-269.
32. Yen, P.M. 2001. Physiological and molecular basis of thyroid hormone action. Physiol. Rev. 81: 1097-1142.
33. Zhang, J. and Lazar, M.A. 2000. The mechanism of action of thyroid hormones. Annu. Rev. Physiol. 62: 439-466.