Crystal structure of bacterial haem importer complex in the inward-facing conformation.
Crystal structure of bacterial haem importer complex in the inward-facing conformation.
复制标题
DOI：
10.1038/ncomms13411
复制
发表时间：
2016-11-10
影响因子：
16.6
通讯作者：
Sugimoto, Hiroshi
中科院分区：
文献类型：
--
作者：
Naoe, Youichi;Nakamura, Nozomi;Doi, Akihiro;Sawabe, Mia;Nakamura, Hiro;Shiro, Yoshitsugu;Sugimoto, Hiroshi
病原菌从宿主组织的血红素中去除铁，并将其用作许多酶的催化中心。病原菌对血红素的摄取是由膜整合血红素输入器促进的，该输入器属于II型ATP结合盒（ABC）转运体。在这里，我们提出的晶体结构伯克霍尔德菌cenocepacia血红素进口商BhuUV与周质血红素结合蛋白BhuT和BhuT的情况下。这些结构的跨膜螺旋显示出向内的构象，其中血红素转运途径的细胞质门是完全打开的。由于这种构象是在血红素和核苷酸的形式，BhuUV-T的结构提供了易位后的状态和丢失的一块在运输周期的II型进口商。结构比较报告的血红素进口商直系同源物HmuUV从鼠疫耶尔森氏菌的面向外的构象提供了机制的见解，在血红素运输周期的构象转变和血红素分泌。 病原菌从ABC血红素转运蛋白输入的血红素辅因子中获得铁。在这里，作者提出的晶体结构伯克霍尔德菌cenocepacia血红素进口商BhuUV与和没有血红素结合蛋白BhuT，收集血红素进口的催化循环的机械见解。
Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding cassette (ABC) transporter. Here we present crystal structures of Burkholderia cenocepacia haem importer BhuUV complexed with the periplasmic haem-binding protein BhuT and in the absence of BhuT. The transmembrane helices of these structures show an inward-facing conformation, in which the cytoplasmic gate of the haem translocation pathway is completely open. Since this conformation is found in both the haem- and nucleotide-free form, the structure of BhuUV-T provides the post-translocation state and the missing piece in the transport cycle of the type II importer. Structural comparison with the outward-facing conformation reported for the haem importer ortholog HmuUV from Yersenia pestis gives mechanistic insights into conformational transitions and haem secretion during the haem transport cycle. Pathogenic bacteria acquire iron from heme cofactors imported by ABC heme transporters. Here the authors present crystal structures of Burkholderia cenocepacia heme importer BhuUV with and without the heme-binding protein BhuT, gathering mechanistic insight into the catalytic cycle of heme import.
登录
查看更多内容
影响因子：
56.9
作者：
Locher, KP;Lee, AT;Rees, DC
通讯作者：
Rees, DC
影响因子：
64.8
作者：
Oldham, Michael L.;Khare, Dheeraj;Chen, Jue
通讯作者：
Chen, Jue
影响因子：
64.8
作者：
Korkhov, Vladimir M.;Mireku, Samantha A.;Locher, Kaspar P.
通讯作者：
Locher, Kaspar P.
影响因子：
16.8
作者：
Korkhov, Vladimir M.;Mireku, Samantha A.;Locher, Kaspar P.
通讯作者：
Locher, Kaspar P.
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K