کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5913613 1162695 2016 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structure of γ-tubulin small complex based on a cryo-EM map, chemical cross-links, and a remotely related structure
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
Structure of γ-tubulin small complex based on a cryo-EM map, chemical cross-links, and a remotely related structure
چکیده انگلیسی

Modeling protein complex structures based on distantly related homologues can be challenging due to poor sequence and structure conservation. Therefore, utilizing even low-resolution experimental data can significantly increase model precision and accuracy. Here, we present models of the two key functional states of the yeast γ-tubulin small complex (γTuSC): one for the low-activity “open” state and another for the higher-activity “closed” state. Both models were computed based on remotely related template structures and cryo-EM density maps at 6.9 Å and 8.0 Å resolution, respectively. For each state, extensive sampling of alignments and conformations was guided by the fit to the corresponding cryo-EM density map. The resulting good-scoring models formed a tightly clustered ensemble of conformations in most regions. We found significant structural differences between the two states, primarily in the γ-tubulin subunit regions where the microtubule binds. We also report a set of chemical cross-links that were found to be consistent with equilibrium between the open and closed states. The protocols developed here have been incorporated into our open-source Integrative Modeling Platform (IMP) software package (http://integrativemodeling.org), and can therefore be applied to many other systems.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 194, Issue 3, June 2016, Pages 303-310
نویسندگان
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