NMR Model of PrgI-SipD Interaction and Its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System
文献类型：期刊论文
| 作者 | Rathinavelan, Thenmalarchelvi1; Lara-Tejero, Maria2; Lefebre, Matthew2; Chatterjee, Srirupa1; McShan, Andrew C.1; Guo, Da-Chuan3; Tang, Chun3; Galan, Jorge E.2; De Guzman, Roberto N.1 |
| 刊名 | JOURNAL OF MOLECULAR BIOLOGY
 |
| 出版日期 | 2014-08-12 |
| 卷号 | 426期号:16页码:2958-2969 |
| 关键词 | Salmonella type III secretion SipD Prgl NMR |
| 英文摘要 | Salmonella and other pathogenic bacteria use the type III secretion system (T3SS) to inject virulence proteins into human cells to initiate infections. The structural component of the T3SS contains a needle and a needle tip. The needle is assembled from Prgl needle protomers and the needle tip is capped with several copies of the SipD tip protein. How a tip protein docks on the needle is unclear. A crystal structure of a Prgl SipD fusion protein docked on the Prgl needle results in steric clash of SipD at the needle tip when modeled on the recent atomic structure of the needle. Thus, there is currently no good model of how SipD is docked on the Prgl needle tip. Previously, we showed by NMR paramagnetic relaxation enhancement (PRE) methods that a specific region in the SipD coiled coil is the binding site for Prgl. Others have hypothesized that a domain of the tip protein-the N-terminal alpha-helical hairpin has to swing away during the assembly of the needle apparatus. Here, we show by PRE methods that a truncated form of SipD lacking the alpha-helical hairpin domain binds more tightly to Prgl. Further, PRE-based structure calculations revealed multiple Prgl binding sites on the SipD coiled coil. Our PRE results together with the recent NMR-derived atomic structure of the Salmonella needle suggest a possible model of how SipD might dock at the Prgl needle tip. SipD and Prgl are conserved in other bacterial T3SSs; thus, our results have wider implication in understanding other needle-tip complexes. (C) 2014 Elsevier Ltd. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | PROTEIN SECRETION ; SHIGELLA-FLEXNERI ; BURKHOLDERIA-PSEUDOMALLEI ; IPAD ; TYPHIMURIUM ; IDENTIFICATION ; ENHANCEMENT ; INJECTISOME ; INSIGHTS ; COMPLEX |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000340327500005 |
| 公开日期 | 2015-07-14 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/1444]  |
| 专题 | 武汉物理与数学研究所_磁共振应用研究部 |
| 作者单位 | 1.Univ Kansas, Dept Mol Biosci, Lawrence, KS 66045 USA 2.Yale Univ, Sch Med, Dept Microbial Pathogenesis, New Haven, CT 06536 USA 3.Chinese Acad Sci, Wuhan Inst Phys & Math, State Key Lab Magnet Resonance & Atom Mol Phys, Key Lab Magnet Resonance Biol Syst, Wuhan 430071, Hubei Province, Peoples R China |
| 推荐引用方式 GB/T 7714 | Rathinavelan, Thenmalarchelvi,Lara-Tejero, Maria,Lefebre, Matthew,et al. NMR Model of PrgI-SipD Interaction and Its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System[J]. JOURNAL OF MOLECULAR BIOLOGY,2014,426(16):2958-2969. |
| APA | Rathinavelan, Thenmalarchelvi.,Lara-Tejero, Maria.,Lefebre, Matthew.,Chatterjee, Srirupa.,McShan, Andrew C..,...&De Guzman, Roberto N..(2014).NMR Model of PrgI-SipD Interaction and Its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System.JOURNAL OF MOLECULAR BIOLOGY,426(16),2958-2969. |
| MLA | Rathinavelan, Thenmalarchelvi,et al."NMR Model of PrgI-SipD Interaction and Its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System".JOURNAL OF MOLECULAR BIOLOGY 426.16(2014):2958-2969. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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