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2002 | 49 | 2 |

Tytuł artykułu

A comparison between the crystal and solution structures of Escherichia coli asparaginase II

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The small angle X-ray scattering (SAXS) pattern of the homotetrameric aspa­raginase II from Escherichia coli was measured in solution in conditions resembling those in which its crystal form was obtained and compared with that calculated from the crystallographic model. The radius of gyration measured by SAXS is about 5% larger and the maximum dimension in the distance distribution function about 12% larger than the corresponding value calculated from the crystal structure. A compari­son of the experimental and calculated distance distribution functions suggests that the overall quaternary structure in the crystal and in solution are similar but that the homotetramer is less compact in solution than in the crystal.

Wydawca

-

Rocznik

Tom

49

Numer

2

Opis fizyczny

p.509-513,fig.

Twórcy

autor
  • Adam Mickiewicz University, Umultowska 85, 61-614 Poznan, Poland
autor

Bibliografia

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  • Boulin CJ, Kempf R, Gabriel A, Koch MHJ. (1988) Data acquisition systems for linear and area X-ray detectors using delay line readout. Nucl Instrum Methods Phys Res.; A269: 312-20.
  • Bu Z, Koide S, Engelman DM. (1998) A solution SAXS study of Borrelia burgdorferi OspA a protein containing a single- layer beta-sheet. Protein Sci.; 7: 2681-3.
  • Chakrabarti R. (1997) L-Asparaginase perspectives on the mechanisms of action and resistance. Int J Pediatr Hematol Oncol.; 4: 597-611.
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  • Janowski R, Kozak M, Jankowska E, Grzonka Z, Grubb A, Abrahamson M, Jaskolski M. (2001) Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat Struct Biol.; 8: 316-20.
  • Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A. (2001) Structures of two highly homologous bacterial L- asparaginases: a case of enantiomorphic space groups. Acta Crystallogr D Biol Crystallogr.; 57: 369-77.
  • Koch MHJ, Bordas J. (1983) X-Ray diffraction and scattering on disordered systems using synchrotron radiation. Nucl Instrum Methods.; 208: 461-9.
  • Kozak M, Jaskolski M. (2000) Crystallization and preliminary crystallographic studies of a new crystal form of Escherichia coliL-asparaginase II (S58A mutant) Acta Crystallogr D Biol Crystallogr.; 56: 509-11.
  • Kozak M, Jaskolski M, Rohm KH. (2000) Preliminary crystallographic studies of Y25F mutant of periplasmic Escherichia coli L-asparaginase Acta Biochim Polon.; 47: 807-14.
  • Kozak M, Borek D, Janowski R, Jaskolski M. (2002) Crystallization and preliminary crystallographic studies of five crystal forms of Escherichia coli L-asparaginase II (Asp90Glu mutant) Acta Crystallogr D Biol Crystallogr.; 58: 130-2.
  • Lindqvist Y, Schneider G, Ermler U, Sundstrom M. (1992) Three-dimensional structure of transketolase, a thiamine diphosphate-dependent enzyme, at 2.5 A resolution. EMBO J.; 11: 2373-9.
  • Lubkowski J, Wlodawer A, Housset D, Weber IT, Ammon HL, Murphy KC, Swain AL. (1994) Refined crystal structure of Acinebacter glutaminaficans glutaminase-asparaginase. Acta Crystallogr D Biol Crystallogr.; 50, 826-32.
  • Murthy NS, Knox JR. (1976) Small-angle X-ray scattering studies of Escherichia coli L-asparaginase. JMol Biol.; 105: 567-75.
  • Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A. (1996) A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant. FEBS Lett.; 390: 211-6.
  • Semenyuk AV, Svergun DI. (1991) GNOM — A program package for small-angle scattering data processing. J Appl Cryst.; 24: 537-40.
  • Svergun DI, Barberato D, Koch MHJ. (1995) CRYSOL — a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates JAppl Cryst; 28: 768-73.
  • Svergun DI, Burkhardt N, Skov Pedersen J, Koch MHJ, Volkov VV, Kozin MB, Meervink W, Stuhrmann HB, Diedrich G, Nierhaus KH. (1997) Solution scattering structural analysis of the 70 S Escherichia coli ribosome by contrast variation. J Mol Biol.; 271: 588-601, 602-18.
  • Svergun DI, Petoukhov MV, Koch MHJ, Konig S. (2000) Crystal versus solution structures of thiamine diphosphate- dependent enzymes. J Biol Chem.; 275: 297-302.
  • Swain AL, Jaskolski M, Housset D, Rao JKM, Wlodawer A. (1993) Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc Natl Acad Sci U S A.; 90: 1474-8.

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Bibliografia

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