The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions
Radiation-induced damage to protein crystals during X-ray diffraction data collection is a major impediment to obtaining accurate structural information on macromolecules. Some of the specific impairments that are inflicted upon highly brilliant X-ray irradiation are metal-ion reduction, disulfide-b...
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doaj-feb17c3b6f0b4c2fa74a305cabed13f42020-11-25T02:43:32ZengInternational Union of CrystallographyIUCrJ2052-25252020-09-017582583410.1107/S2052252520008520lz5035The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactionsRajasri Bhattacharyya0Jesmita Dhar1Shubhra Ghosh Dastidar2Pinak Chakrabarti3Manfred S. Weiss4Department of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, IndiaDepartment of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, IndiaDivision of Bioinformatics, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, IndiaDepartment of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, IndiaMacromolecular Crystallography (HZB-MX), Helmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Strasse 15, D-12489 Berlin, GermanyRadiation-induced damage to protein crystals during X-ray diffraction data collection is a major impediment to obtaining accurate structural information on macromolecules. Some of the specific impairments that are inflicted upon highly brilliant X-ray irradiation are metal-ion reduction, disulfide-bond cleavage and a loss of the integrity of the carboxyl groups of acidic residues. With respect to disulfide-bond reduction, previous results have indicated that not all disulfide bridges are equally susceptible to damage. A careful analysis of the chemical environment of disulfide bonds in the structures of elastase, lysozyme, acetylcholinesterase and other proteins suggests that S—S bonds which engage in a close contact with a carbonyl O atom along the extension of the S—S bond vector are more susceptible to reduction than the others. Such an arrangement predisposes electron transfer to occur from the O atom to the disulfide bond, leading to its reduction. The interaction between a nucleophile and an electrophile, akin to hydrogen bonding, stabilizes protein structures, but it also provides a pathway of electron transfer to the S—S bond, leading to its reduction during exposure of the protein crystal to an intense X-ray beam. An otherwise stabilizing interaction can thus be the cause of destabilization under the condition of radiation exposure.http://scripts.iucr.org/cgi-bin/paper?S2052252520008520radiation damagedisulfide bondss...o interactionsquantum-chemical calculationsnboelectron transfer |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Rajasri Bhattacharyya Jesmita Dhar Shubhra Ghosh Dastidar Pinak Chakrabarti Manfred S. Weiss |
spellingShingle |
Rajasri Bhattacharyya Jesmita Dhar Shubhra Ghosh Dastidar Pinak Chakrabarti Manfred S. Weiss The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions IUCrJ radiation damage disulfide bonds s...o interactions quantum-chemical calculations nbo electron transfer |
author_facet |
Rajasri Bhattacharyya Jesmita Dhar Shubhra Ghosh Dastidar Pinak Chakrabarti Manfred S. Weiss |
author_sort |
Rajasri Bhattacharyya |
title |
The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions |
title_short |
The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions |
title_full |
The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions |
title_fullStr |
The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions |
title_full_unstemmed |
The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions |
title_sort |
susceptibility of disulfide bonds towards radiation damage may be explained by s...o interactions |
publisher |
International Union of Crystallography |
series |
IUCrJ |
issn |
2052-2525 |
publishDate |
2020-09-01 |
description |
Radiation-induced damage to protein crystals during X-ray diffraction data collection is a major impediment to obtaining accurate structural information on macromolecules. Some of the specific impairments that are inflicted upon highly brilliant X-ray irradiation are metal-ion reduction, disulfide-bond cleavage and a loss of the integrity of the carboxyl groups of acidic residues. With respect to disulfide-bond reduction, previous results have indicated that not all disulfide bridges are equally susceptible to damage. A careful analysis of the chemical environment of disulfide bonds in the structures of elastase, lysozyme, acetylcholinesterase and other proteins suggests that S—S bonds which engage in a close contact with a carbonyl O atom along the extension of the S—S bond vector are more susceptible to reduction than the others. Such an arrangement predisposes electron transfer to occur from the O atom to the disulfide bond, leading to its reduction. The interaction between a nucleophile and an electrophile, akin to hydrogen bonding, stabilizes protein structures, but it also provides a pathway of electron transfer to the S—S bond, leading to its reduction during exposure of the protein crystal to an intense X-ray beam. An otherwise stabilizing interaction can thus be the cause of destabilization under the condition of radiation exposure. |
topic |
radiation damage disulfide bonds s...o interactions quantum-chemical calculations nbo electron transfer |
url |
http://scripts.iucr.org/cgi-bin/paper?S2052252520008520 |
work_keys_str_mv |
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