The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook

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• 作者：Fré ; dé ; ric V. Stanger¹ ; ² ; ⁵ ; ⁶ ; Tjaart A.P. de Beer¹ ; ⁵ ; David M. Dranow³ ; ⁴ ; ⁵ ; Tilman Schirmer² ; ^{tilman.schirmer@unibas.ch} ; Isabelle Phan³ ; Christoph Dehio¹ ; ⁷ ; ^{christoph.dehio@unibas.ch}
• 关键词：secretion system ; secretion signal ; type IV secretion system (T4SS) ; bacterial conjugation ; novel fold ; BID domain ; Bartonella effector proteins (Beps) ; relaxases ; four-helix bundle
• 刊名：Structure
• 出版年：2017
• 出版时间：3 January 2017
• 年：2017
• 卷：25
• 期：1
• 页码：203-211
• 全文大小：3813 K
• 卷排序：25

文摘

BID domains share a novel fold with a compact four-helix bundle and a hook The rigid fold is determined by a conserved core of hydrophobic amino acids Charged surface areas and few exposed residues are preserved Low surface conservation facilitates the evolution of secondary functions