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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):973-5. doi: 10.1107/S1744309106033100. Epub 2006 Sep 19.
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ATP-induced FliI hexamerization facilitates bacterial flagellar protein export.ATP诱导的FliI六聚化促进细菌鞭毛蛋白输出。
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Bacterial rotary export ATPases are allosterically regulated by the nucleotide second messenger cyclic-di-GMP.细菌旋转输出ATP酶受核苷酸第二信使环二鸟苷酸的变构调节。
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本文引用的文献

1
Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region.细菌鞭毛ATP酶FliI的寡聚化受其极端N端区域的控制。
J Mol Biol. 2006 Jul 7;360(2):510-9. doi: 10.1016/j.jmb.2006.05.010. Epub 2006 May 19.
2
Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori.幽门螺杆菌鞭毛输出蛋白FliI和FliH之间相互作用的分子基础
J Biol Chem. 2006 Jan 6;281(1):508-17. doi: 10.1074/jbc.M507238200. Epub 2005 Oct 31.
3
Chaperone release and unfolding of substrates in type III secretion.伴侣蛋白释放与III型分泌中底物的解折叠
Nature. 2005 Oct 6;437(7060):911-5. doi: 10.1038/nature03992.
4
Type III flagellar protein export and flagellar assembly.III型鞭毛蛋白输出与鞭毛组装
Biochim Biophys Acta. 2004 Nov 11;1694(1-3):207-17. doi: 10.1016/j.bbamcr.2004.04.005.
5
Self-assembly and type III protein export of the bacterial flagellum.细菌鞭毛的自组装及III型蛋白质输出
J Mol Microbiol Biotechnol. 2004;7(1-2):5-17. doi: 10.1159/000077865.
6
Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export.鞭毛III型蛋白输出过程中胞质伴侣-底物复合物在膜ATP酶处的对接。
Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3945-50. doi: 10.1073/pnas.0307223101. Epub 2004 Mar 4.
7
The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH.在缺乏其调节因子FliH的情况下，ATP酶FliI可与III型鞭毛蛋白输出装置相互作用。
J Bacteriol. 2003 Jul;185(13):3983-8. doi: 10.1128/JB.185.13.3983-3988.2003.
8
Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly.FliI ATP酶的寡聚化与激活对于细菌鞭毛组装至关重要。
Mol Microbiol. 2003 Jun;48(5):1349-55. doi: 10.1046/j.1365-2958.2003.03506.x.
9
How bacteria assemble flagella.细菌如何组装鞭毛。
Annu Rev Microbiol. 2003;57:77-100. doi: 10.1146/annurev.micro.57.030502.090832. Epub 2003 May 1.
10
Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway.沙门氏菌FliH的分子剖析，FliH是ATP酶FliI和III型鞭毛蛋白输出途径的调节因子。
Mol Microbiol. 2002 Aug;45(4):967-82. doi: 10.1046/j.1365-2958.2002.03047.x.

鼠伤寒沙门氏菌FliI（III型鞭毛蛋白输出装置的ATP酶成分）的结晶及初步X射线分析。

Crystallization and preliminary X-ray analysis of Salmonella FliI, the ATPase component of the type III flagellar protein-export apparatus.

作者信息

Minamino Tohru, Imada Katsumi, Tahara Aiko, Kihara May, Macnab Robert M, Namba Keiichi

机构信息

Dynamic NanoMachine Project, ICORP, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):973-5. doi: 10.1107/S1744309106033100. Epub 2006 Sep 19.

DOI:10.1107/S1744309106033100
PMID:17012787
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2225186/
Abstract

Most of the structural components making up the bacterial flagellum are translocated through the central channel of the growing flagellar structure by the type III flagellar protein-export apparatus in an ATPase-driven manner and are assembled at the growing end. FliI is the ATPase that drives flagellar protein export using the energy of ATP hydrolysis. FliI forms an oligomeric ring structure in order to attain maximum ATPase activity. In this study, FliI(Delta1-18), an N-terminally truncated variant of FliI lacking the first 18 residues, was purified and crystallized. Crystals were obtained using the hanging-drop vapour-diffusion technique with PEG 8000 as a precipitant. FliI(Delta1-18) crystals grew in the monoclinic space group P2(1), with unit-cell parameters a = 48, b = 73, c = 126 A, beta = 94 degrees, and diffracted to 2.4 A resolution. Anomalous difference Patterson maps of Os-derivative and Pt-derivative crystals showed significant peaks in their Harker sections, indicating that both derivatives are suitable for structure determination.

摘要

构成细菌鞭毛的大多数结构成分通过III型鞭毛蛋白输出装置以ATP酶驱动的方式转运穿过正在生长的鞭毛结构的中央通道，并在生长末端组装。FliI是利用ATP水解能量驱动鞭毛蛋白输出的ATP酶。FliI形成寡聚环结构以获得最大的ATP酶活性。在本研究中，纯化并结晶了FliI(Delta1-18)，它是FliI的N端截短变体，缺少前18个残基。使用悬滴气相扩散技术，以聚乙二醇8000作为沉淀剂获得晶体。FliI(Delta1-18)晶体在单斜空间群P2(1)中生长，晶胞参数为a = 48，b = 73，c = 126 Å，β = 94°，衍射分辨率为2.4 Å。Os衍生物和Pt衍生物晶体的反常差值帕特森图在其哈克截面显示出明显的峰，表明这两种衍生物都适合用于结构测定。