Circular permutation of βB2-crystallin changes the hierarchy of domain assembly

Protein Science

Volumn 7, Issue 6, 1998, Pages 1280-1285

  Wright, G ^a   Basak, A K ^a   Wieligmann, K ^b   Mayr, E M ^b   Slingsby, C ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Circular permutation; Domain swapping; Domain swivelling; Eye lens protein; Quaternary structure; crystallin

Indexed keywords

BETA CRYSTALLIN; DIMER; GAMMA CRYSTALLIN; LENS PROTEIN; POLYPEPTIDE; TETRAMER; CRYSTALLIN;

ARTICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; DIMERIZATION; MACROMOLECULE; MOLECULAR GENETICS; RAT; X RAY CRYSTALLOGRAPHY;

ANIMALS; CRYSTALLINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; RATS;

EID: 0031595862     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070602     Document Type: Article

References (29)

1. Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, Blundell TL, Slingsby C. 1990. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature 347:776-780.
2. Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping - A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
3. Berbers GAM, Hoekman WA, Bloemendal H, de Jong WW, Kleinschmidt T, Braunitzer G. 1984. Homology between the primary structures of the major bovine β-crystallin chains. Eur J Biochem 139:467-479.
4. Bergdoll M, Remy M-H, Cagnon C, Masson J-M, Dumas P. 1997. Proline-dependent oligomerization with arm exchange. Structure 5:391-401.
5. Blundell T, Lindley P, Miller L, Moss D, Slingsby C, Tickle I, Tumell B, Wistow G. 1981. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature 289:771-777.
6. Brunger AT. 1992. Free R-value - A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475.
7. CCP4 - Collaborative Computational Project, Number 4. 1994. The CCP4 suite -Programs for protein crystallography. Acta Crystallogr D50:760-763.
8. Clout NJ, Slingsby C, Wistow GJ. 1997. An eye on crystallins. Nat Struct Biol 4:685.
9. de Jong WW, Lubsen NH, Kraft HJ. 1994. Molecular evolution of the eye lens. Prog Ret Eye Res 13:391-442.
10. Driessen HPC, Bax B, Slingsby C, Lindley PF, Mahadevan D, Moss DS, Tickle IJ. 1991 Structure of oligomeric βB2-crystallin: An application of the T2 translation function to an asymmetric unit containing two dimers. Acta Crystallogr B47:987-997.
11. Evans SV. 1993. SETOR - Hardware highlighted 3-dimensional model representations of macromolecules. J Mol Graphics 11:134-138.
12. Gilbert W. 1987. The exon theory of genes. Cold Spring Harbor Symp Quant Biol 52:901-905.
13. Heringa J, Taylor WR. 1997. Three-dimensional domain duplication, swapping and stealing. Curr Opin Struct Biol 7:416-421.
14. Hope JN, Chen H-C, Hejtmancik JF. 1994. Aggregation of βA3-crystallin is independent of the specific sequence of the domain connecting peptide. J Biol Chem 269:21141-21145.
15. Lampi KJ, Ma Z, Shih M, Shearer TR, Smith JB, Smith DL, David LL. 1997. Sequence analysis of βA3, βB3, and βA4 crystallins completes the identification of the major proteins in young human lens. J Biol Chem 272:2268-2275.
16. Lindqvist Y, Schneider G. 1997. Circular permutations of natural protein sequences: Structural evidence. Curr Struct Biol 7:422-427.
17. Mayr E-M, Jaenicke R, Glockshuber R. 1994. Domain interactions and connecting peptides in lens crystallins. J Biol Mol 235:84-88.
18. Navaza J. 1994. AMORE: An automated package for molecular replacement. Acta Crystallogr A50:157-163.
19. Nicholls A, Bharadwaj R, Honig B. 1993. GRASP - Graphical representation and analysis of surface properties. Biophys J 64:166.
20. Norledge BV, Mayr E-M, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HPC. 1996. The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins. Nat Struct Biol 3:267-274.
21. Otwinowski Z. 1993. Proceedings of the CCP4 Study Weekend. Sawyer L, Isaacs N, Bailey S, eds. Daresbury, UK: SERC, Daresbury Laboratory. pp 56-62.
22. Ponting CP, Russell RB. 1995. Swaposins - Circular permutations within genes encoding saposin homologs. Trends Biochem Sci 20:179-180.
23. Slingsby C, Bateman OA. 1990. Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of β-crystallins favor heterologous association. Biochemistry 29:6592-6599.
24. Slingsby C, Bateman OA. 1994. Formation and crystallization of the eye lens heterodimer βB2-βB3-crystallin. Exp Eye Res 58:761-764.
25. Trinkl S. 1995. PhD thesis, University of Regensburg.
26. Trinkl S, Glockshuber R, Jaenicke R. 1994. Dimerization of βB2-crystallin: The role of the linker peptide and the N-and C-terminal extensions. Protein Sci 3:1392-1400.
27. Wieligmann K, Norledge B, Jaenicke R, Mayr E-M. 1998. J Mol Biol. In press.
28. Wistow GJ, Piatigorsky J. 1988. Lens crystallins: The evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem 57:479-504.
29. Zarina S, Slingsby C, Jaenicke R, Zaidi ZH, Driessen H, Srinivasan N. 1994. Three-dimensional model and quaternary structure of the human eye lens protein γS-crystallin based on β-and γ-crystallin X-ray coordinates and ultracentrifugation. Protein Sci 3:1840-1846.