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Titolo:
Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes
Autore:
Weik, M; Ravelli, RBG; Silman, I; Sussman, JL; Gros, P; Kroon, J;
Indirizzi:
Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 ruct, IL-76100 Rehovot, Israel Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 biol, IL-76100 Rehovot, Israel European Mol Biol Lab, Grenoble Outstn, F-38042 Grenoble, France European Mol Biol Lab Grenoble France F-38042 , F-38042 Grenoble, France Univ Utrecht, Bijvoet Ctr Biomol Res, Dept Crystal & Struct Chem, NL-3584 CH Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3584 CH 3584 CH Utrecht, Netherlands
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 10, volume: 10, anno: 2001,
pagine: 1953 - 1961
SICI:
0961-8368(200110)10:10<1953:SPDNTS>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
X-RAY-DIFFRACTION; NEUTRON-SCATTERING; GAMMA-RADIOLYSIS; PULSE-RADIOLYSIS; DAMAGE; LYSOZYME; MOTIONS; WATER; ACETYLCHOLINESTERASE; FRAGMENTATION;
Keywords:
temperature-dependent protein crystallography; dynamical transition in proteins; solvent glass transition; radiation damage; disulfide; acetylcholinesterase; enzyme radiation-inactivation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Weik, M Inst Biol Struct, Lab Mol Biophys, 41 Rue Jules Horowitz, F-38027 Grenoble1, France Inst Biol Struct 41 Rue Jules Horowitz Grenoble France 1, France
Citazione:
M. Weik et al., "Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes", PROTEIN SCI, 10(10), 2001, pp. 1953-1961

Abstract

The nature of the dynamical coupling between a protein and its surroundingsolvent is an important, yet open issue. Here we used temperature-dependent protein crystallography to study structural alterations that arise in theenzyme acetylcholinesterase upon X-ray irradiation at two temperatures: below and above the glass transition of the crystal solvent. A buried disulfide bond, a buried cysteine, and solvent exposed methionine residues show drastically increased radiation damage at 155 K, in comparison to 100 K. Additionally, the irradiation-induced unit cell volume increase is linear at 100 K, but not at 155 K, which is attributed to the increased solvent mobility at 155 K. Most importantly, we observed conformational changes in the catalytic triad at the active site at 155 K but not at 100 K. These changes lead to an inactive catalytic triad conformation and represent, therefore, the observation of radiation-inactivation of an enzyme at the atomic level. Our results show that at 155 K, the protein has acquired-at least locally-sufficient conformational flexibility to adapt to irradiation-induced alterations in the conformational energy landscape. The increased protein flexibility may be a direct consequence of the solvent glass transition, which expresses as dynamical changes in the enzyme's environment. Our results reveal the importance of protein and solvent dynamics in specific radiation damageto biological macromolecules, which in turn can serve as a tool to study protein flexibility and its relation to changes in a protein's environment.

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Documento generato il 04/04/20 alle ore 12:19:12