Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization

التفاصيل البيبلوغرافية
العنوان: Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization
المؤلفون: Susan J. Firbank, Christopher Dennison, Mark J. Banfield, Pedro M. Matias, Hualing Mi, Peter B. Crowley
المصدر: Biochemistry. 47:6583-6589
بيانات النشر: American Chemical Society (ACS), 2008.
سنة النشر: 2008
مصطلحات موضوعية: Models, Molecular, Protein Conformation, Chemistry, Supramolecular chemistry, Crystallography, X-Ray, Cyanobacteria, Biochemistry, Acceptor, Electron transport chain, Protein Structure, Secondary, Recombinant Proteins, Electron Transport, Crystal, Crystallography, Electron transfer, Bacterial Proteins, Side chain, Molecule, Protein Multimerization, Crystallization, Plastocyanin, Copper, Protein Binding
الوصف: The accepted view of interprotein electron transport involves molecules diffusing between donor and acceptor redox sites. An emerging alternative hypothesis is that efficient long-range electron transport can be achieved through proteins arranged in supramolecular assemblies. In this study, we have investigated the crystal packing interfaces in three crystal forms of plastocyanin, an integral component of the photosynthetic electron transport chain, and discuss their potential relevance to in vivo supramolecular assemblies. Symmetry-related protein chains within these crystals have Cu-Cu separations of
تدمد: 1520-4995
0006-2960
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7648a85e9f1dafaac5e2cb3f7a758cdeTest
https://doi.org/10.1021/bi800125hTest
رقم الانضمام: edsair.doi.dedup.....7648a85e9f1dafaac5e2cb3f7a758cde
قاعدة البيانات: OpenAIRE