Flexibility in the Periplasmic Domain of BamA Is Important for Function

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• 作者：Lisa R. Warner¹ ; ² ; Petia Z. Gatzeva-Topalova¹ ; Pamela A. Doerner¹ ; Arthur Pardi¹ ; ^{arthur.pardi@colorado.edu} ; Marcelo C. Sousa¹ ; ³ ; ^{marcelo.sousa@colorado.edu}
• 关键词：Escherichia coli ; BamA ; residual dipolar couplings ; interdomain flexibility ; POTRA ; disulfide crosslinking
• 刊名：Structure
• 出版年：2017
• 出版时间：3 January 2017
• 年：2017
• 卷：25
• 期：1
• 页码：94-106
• 全文大小：3625 K
• 卷排序：25

文摘

BamA with a transmembrane β-barrel and soluble POTRA motifs mediates OMP biogenesis NMR relaxation studies show POTRA1–2 is flexibly linked to POTRA3–5 in BamA Residual dipolar couplings indicate POTRA1–2 and POTRA4–5 behave as rigid species Disulfides that restrict POTRA2–3 flexibility impair in vivo function of BamA