• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

利用400 kV电子冷冻显微镜对鲎精子顶体丝的三维结构进行研究。

Three-dimensional structure of the acrosomal filament of Limulus sperm by 400 kV electron cryomicroscopy.

作者信息

Schmid M F, Jakana J, Matsudaira P, Chiu W

机构信息

Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA.

出版信息

Biophys J. 1995 Apr;68(4 Suppl):8S-11S.

PMID:7787112
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1281851/
Abstract

The acrosomal bundle of Limulus sperm was imaged by electron cryomicroscopy, and the three-dimensional structure of a filament computationally isolated from the bundle was determined by helical image reconstruction. The actin model of Holmes was fit into the map, and its interactions with scruin, the actin-binding and cross-linking protein, were studied. Scruin binds to two consecutive actins along the helix via subdomains 1 and 3. These interactions involve helix-loop-beta motifs that are present in both actin subdomains (in different monomers) in positions available for binding by the same scruin molecule as it wraps around the actin. Taking first the structural motif homology and then looking for sequence pattern similarities, a stretch of 12 out of 20 matches in hydrophobicity is found. Scruin itself has been found to have an internal tandem homology.

摘要

通过电子冷冻显微镜对鲎精子的顶体束进行成像,并通过螺旋图像重建确定从该束中计算分离出的细丝的三维结构。将福尔摩斯的肌动蛋白模型拟合到图谱中,并研究其与肌动蛋白结合和交联蛋白scruin的相互作用。Scruin通过亚结构域1和3沿着螺旋与两个连续的肌动蛋白结合。这些相互作用涉及肌动蛋白亚结构域(在不同单体中)中存在的螺旋-环-β基序,当scruin分子围绕肌动蛋白缠绕时,这些基序处于可被同一scruin分子结合的位置。首先考虑结构基序同源性,然后寻找序列模式相似性,发现在20个匹配中有12个在疏水性上相似。已发现scruin本身具有内部串联同源性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c0f/1281851/99f55e69a013/biophysj00062-0022-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c0f/1281851/accbab1cb7a4/biophysj00062-0021-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c0f/1281851/99f55e69a013/biophysj00062-0022-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c0f/1281851/accbab1cb7a4/biophysj00062-0021-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c0f/1281851/99f55e69a013/biophysj00062-0022-a.jpg

相似文献

1
Three-dimensional structure of the acrosomal filament of Limulus sperm by 400 kV electron cryomicroscopy.利用400 kV电子冷冻显微镜对鲎精子顶体丝的三维结构进行研究。
Biophys J. 1995 Apr;68(4 Suppl):8S-11S.
2
Three-dimensional structure of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-beta motifs in actin.鲎顶体束中单个细丝的三维结构:丝氨酸蛋白酶抑制蛋白与肌动蛋白中的同源螺旋-环-β基序结合。
J Cell Biol. 1994 Feb;124(3):341-50. doi: 10.1083/jcb.124.3.341.
3
A 13-A map of the actin-scruin filament from the limulus acrosomal process.来自鲎顶体突的肌动蛋白-血影蛋白丝的13-A图谱。
J Cell Biol. 1993 Oct;123(2):337-44. doi: 10.1083/jcb.123.2.337.
4
The three-dimensional structure of the Limulus acrosomal process: a dynamic actin bundle.鲎顶体突的三维结构:动态肌动蛋白束。
J Mol Biol. 1999 Nov 19;294(1):139-49. doi: 10.1006/jmbi.1999.3222.
5
Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm.鲎精子顶体突中肌动蛋白交联蛋白scruin的序列和结构域组织
J Cell Biol. 1995 Jan;128(1-2):51-60. doi: 10.1083/jcb.128.1.51.
6
A 7-A projection map of frozen, hydrated acrosomal bundle from Limulus sperm.鲎精子冷冻水合顶体束的7-A投影图。
J Struct Biol. 1995 Sep-Oct;115(2):209-13. doi: 10.1006/jsbi.1995.1045.
7
Crystallographic analysis of acrosomal bundle from Limulus sperm.鲎精子顶体束的晶体学分析。
J Mol Biol. 1991 Sep 20;221(2):711-25. doi: 10.1016/0022-2836(91)80082-6.
8
Bending stiffness of a crystalline actin bundle.晶体肌动蛋白束的弯曲刚度。
J Mol Biol. 2004 Mar 19;337(2):255-61. doi: 10.1016/j.jmb.2004.01.028.
9
Imaging frozen, hydrated acrosomal bundle from Limulus sperm at 7 A resolution with a 400 kV electron cryomicroscope.使用400 kV电子冷冻显微镜以7 Å分辨率对鲎精子的冷冻水合顶体束进行成像。
J Mol Biol. 1993 Mar 20;230(2):384-6. doi: 10.1006/jmbi.1993.1155.
10
Crystallographic conformers of actin in a biologically active bundle of filaments.肌动蛋白在具有生物活性的丝状束中的晶体学构象异构体。
J Mol Biol. 2008 Jan 11;375(2):331-6. doi: 10.1016/j.jmb.2007.10.027. Epub 2007 Oct 16.

本文引用的文献

1
Imaging frozen, hydrated acrosomal bundle from Limulus sperm at 7 A resolution with a 400 kV electron cryomicroscope.使用400 kV电子冷冻显微镜以7 Å分辨率对鲎精子的冷冻水合顶体束进行成像。
J Mol Biol. 1993 Mar 20;230(2):384-6. doi: 10.1006/jmbi.1993.1155.
2
kelch encodes a component of intercellular bridges in Drosophila egg chambers.kelch基因编码果蝇卵室中细胞间桥的一个组成部分。
Cell. 1993 Mar 12;72(5):681-93. doi: 10.1016/0092-8674(93)90397-9.
3
A 13-A map of the actin-scruin filament from the limulus acrosomal process.来自鲎顶体突的肌动蛋白-血影蛋白丝的13-A图谱。
J Cell Biol. 1993 Oct;123(2):337-44. doi: 10.1083/jcb.123.2.337.
4
Three-dimensional structure of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-beta motifs in actin.鲎顶体束中单个细丝的三维结构:丝氨酸蛋白酶抑制蛋白与肌动蛋白中的同源螺旋-环-β基序结合。
J Cell Biol. 1994 Feb;124(3):341-50. doi: 10.1083/jcb.124.3.341.
5
Drosophila kelch motif is derived from a common enzyme fold.果蝇kelch基序源自一种常见的酶折叠结构。
J Mol Biol. 1994 Mar 11;236(5):1277-82. doi: 10.1016/0022-2836(94)90056-6.
6
Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm.鲎精子顶体突中肌动蛋白交联蛋白scruin的序列和结构域组织
J Cell Biol. 1995 Jan;128(1-2):51-60. doi: 10.1083/jcb.128.1.51.
7
Atomic model of the actin filament.肌动蛋白丝的原子模型。
Nature. 1990 Sep 6;347(6288):44-9. doi: 10.1038/347044a0.
8
Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.半乳糖氧化酶1.7埃晶体结构揭示的新型硫醚键
Nature. 1991 Mar 7;350(6313):87-90. doi: 10.1038/350087a0.
9
Crystallographic analysis of acrosomal bundle from Limulus sperm.鲎精子顶体束的晶体学分析。
J Mol Biol. 1991 Sep 20;221(2):711-25. doi: 10.1016/0022-2836(91)80082-6.
10
Identification of a novel murine IAP-promoted placenta-expressed gene.一种新型小鼠IAP促进的胎盘表达基因的鉴定。
Nucleic Acids Res. 1991 Jul 11;19(13):3667-72. doi: 10.1093/nar/19.13.3667.