On the domains of T4 phage sliding clamp gp45: An intermolecular crosstalk governs structural stability and biological activity

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• 作者：Manika Indrajit Singh ; Bylapudi Ganesh¹ ; Vikas Jain ; ^{vikas@iiserb.ac.in}
• 关键词：CLC ; clamp loader complex ; BN-PAGE ; Blue-Native polyacrylamide gel electrophoresis ; DTT ; Dithiothreitol ; EDTA ; Ethylenediaminetetraacetic acid
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3300-3310
• 全文大小：1368 K
• 卷排序：1861

文摘

Bacteriophage T4 homotrimeric sliding clamp gp45 is stable only as a trimer. Perturbing interface interaction causes lowering of thermal & chemical stabilities. gp45 adopts ‘molten globule’-like intermediate state during chemical unfolding. N-ter and C-ter domains affect each other's topology by an inter-domain crosstalk. Interactions with CTD scaffold are necessary for gp45 trimerization and NTD folding.