It started off as a Cys, how did it end up like this? Identifying the extent of unmodelled oxidatively modified cysteines within the Protein Data Bank.
Samuel P Foster, Anna J Warren, C Alistair Siebert, Jaswir Basran, Peter C E Moody
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引用次数: 0
Abstract
Radiation damage to macromolecular structures remains a significant challenge for accurate structure solution by X-ray crystallography, leading to incorrect structural and chemical interpretation of the data. Site-specific radiation damage is insidious, typically unidentifiable solely from summary statistics, and is primarily discussed with reference to the predominant forms: disulfide-bond cleavage, metal-centre reduction and decarboxylation of acidic residues. A method is presented for identifying potentially oxidatively damaged cysteines by interrogating the accuracy of the built model within the electron density and the geometry of the difference density peaks surrounding a cysteine. We also highlight that cysteines located within protein active sites or that are in hydrolases are predisposed to this damage.
期刊介绍：
Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them.
Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged.
Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.
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