Exploring the Limits of Sequence and Structure in a Variant βγ-Crystallin Domain of the Protein Absent in Melanoma-1 (AIM1)

Journal of Molecular Biology

Volumn 381, Issue 3, 2008, Pages 509-518

  Aravind, Penmatsa ^a   Wistow, Graeme ^b   Sharma, Yogendra ^a   Sankaranarayanan, Rajan ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

^b NATIONAL EYE INSTITUTE   (United States)

Author keywords

AIM1g1; Greek key motif; Trp corner; Tyr corner; crystallin

Indexed keywords

ABSENT IN MELANOMA 1; BETAGAMMA CRYSTALLIN; CRYSTALLIN; PROTEIN DERIVATIVE;

ARTICLE; CRYSTAL STRUCTURE; GENE SEQUENCE; GENETIC VARIABILITY; MELANOMA; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE;

EUKARYOTA; PROKARYOTA; VERTEBRATA;

EID: 47849100705     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.06.019     Document Type: Article

References (34)

1. Wistow G.J., and Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu. Rev. Biochem. 57 (1988) 479-504
2. Bloemendal H., de Jong W., Jaenicke R., Lubsen N.H., Slingsby C., and Tardieu A. Prog. Biophys. Mol. Biol. 86 (2004) 407-485
3. Jaenicke R., and Slingsby C. Lens crystallins and their microbial homologs: structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36 (2001) 435-499
4. Blundell T.L., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., et al. The molecular structure and stability of the eye lens: X-ray analysis of gamma-crystallin II. Nature 289 (1981) 771-777
5. Wistow G., Turnell B., Summers L., Slingsby C., Moss D., Miller L., et al. X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 Å resolution. J. Mol. Biol. 170 (1983) 175-202
6. Slingsby C., Norledge B., Simpson A., Bateman O.A., Wright G., Driessen H.P.C., et al. X-ray diffraction and structure of crystallins. Prog. Retinal Eye Res. 16 (1997) 3-29
7. Bagby S., Go S., Inouye S., Ikura M., and Chakrabartty A. Equilibrium folding intermediates of a Greek key beta-barrel protein. J. Mol. Biol. 276 (1998) 669-681
8. Antuch W., Guntert P., and Wuthrich K. Ancestral βγ crystallin precursor structure in a killer toxin. Nat. Struct. Biol. 3 (1996) 662-665
9. Ohki S.Y., Kariya E., Hiraga K., Wakamiya A., Isobe T., Oda K., and Kainosho M. NMR structure of Streptomyces killer toxin-like protein, SKLP: further evidence for the wide distribution of single-domain betagamma-crystallin superfamily proteins. J. Mol. Biol. 305 (2001) 109-120
10. Clout N.J., Wistow G., and Slingsby C. An eye on crystallins. Nat. Struct. Biol. 4 (1997) 685
11. Wistow G. Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30 (1990) 140-145
12. Clout N.J., Kretschmar M., Jaenicke R., and Slingsby C. Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens betagamma-crystallin domain fold. Structure 9 (2001) 115-124
13. Hamill J.H., Cota E., Chothia C., and Clarke J. Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul-de-sac. J. Mol. Biol. 295 (2000) 641-649
14. Jobby M.K., and Sharma Y. Calcium-binding crystallins from Yersinia pestis: characterization of two single beta gamma-crystallin domains of a putative exported protein. J. Biol. Chem. 280 (2005) 1209-1216
15. Ray M.E., Wistow G., Su Y.A., Meltzer P.S., and Trent J.M. AIM1, a novel non-lens member of the βγ-crystallin superfamily, is associated with the control of tumorigenicity in human malignant melanoma. Proc. Natl Acad. Sci. USA 94 (1997) 3229-3234
16. Rajini B., Graham C., Wistow G., and Sharma Y. Stability, homodimerization, and calcium-binding properties of a single, variant βγ-crystallin domain of the protein absent in melanoma 1 (AIM1). Biochemistry 42 (2003) 4552-4559
17. Holm L., and Park J. Dalilite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
18. Aravind P., Rajini B., Sharma Y., and Sankaranarayanan R. Crystallization and preliminary X-ray crystallographic investigations on a βγ-crystallin domain of Absent In Melanoma 1 (AIM1), a protein from Homo sapiens. Acta Crystallogr., Sect. F 62 (2006) 282-284
19. Yogavel M., Gill J., Mishra P.C., and Sharma A. SAD phasing of a structure based on co-crystallized iodides using an in-house Cu Kα X-ray source: effects of data redundancy and completeness on structure solution. Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 (2007) 931-934
20. Hanson S.R., Smith D.L., and Smith J.B. Deamidation and disulfide bonding in human lens gamma-crystallins. Exp. Eye Res. 67 (1998) 301-312
21. Skouri-Panet F., Bonneté F., Prat K., Bateman O.A., Lubsen N.H., and Tardieu A. Lens crystallins and oxidation: the special case of gammaS. Biophys. Chem. 89 (2001) 65-76
22. Zauhar R.J., Colbert C.L., Morgan R.S., and Welsh W.J. Evidence for a strong sulfur-aromatic interaction derived from crystallographic data. Biopolymers 53 (2000) 233-248
23. Ohno A., Tate S., Seeram S.S., Hiraga K., Swindells M.B., Oda K., and Kainosho M. NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure. J. Mol. Biol. 282 (1998) 421-433
24. Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11 (1991) 281-296
25. Strynadka N.C., and James M.N. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58 (1989) 951-998
26. Rajini B., Shridas P., Sundari C.S., Muralidhar D., Chandani S., Thomas F., and Sharma Y. Calcium binding properties of gamma-crystallin: calcium ion binds at the Greek key beta gamma-crystallin fold. J. Biol. Chem. 276 (2001) 38464-38471
27. Jobby M.K., and Sharma Y. Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins. FEBS J. 274 (2007) 4135-4147
28. Scandurra R., Consalvi V., Chiaraluce R., Politi L., and Engel P.C. Protein stability in extremophilic archaea. Front. Biosci. 5 (2000) 787-795
29. Vogt G., Woell S., and Argos P. Protein thermostability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269 (1997) 631-643
30. Cooper A. Heat capacity of hydrogen-bonded networks: an alternative view of protein folding thermodynamics. Biophys. Chem. 85 (2000) 25-39
31. Lapatto R., Nalini V., Bax B., Driessen H., Lindley P.F., Blundell T.L., and Slingsby C. High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin. J. Mol. Biol. 222 (1991) 1067-1083
32. Clout N.J., Basak A., Wieligmann K., Bateman O.A., Jaenicke R., and Slingsby C. The N-terminal domain of βB2-crystallin resembles the putative ancestral homodimer. J. Mol. Biol. 304 (2000) 253-257
33. Shimeld S.M., Purkiss A.G., Dirks R.P., Bateman O.A., Slingsby C., and Lubsen N.H. Urochordate betagamma-crystallin and the evolutionary origin of the vertebrate eye lens. Curr. Biol. 15 (2005) 1684-1689
34. Grishin N.V. Fold change in evolution of protein structures. J. Struct. Biol. 134 (2001) 167-185