X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex.

Kawamura K; Yamada T; Kurihara KTamada TKuroki RTanaka ITakahashi HNiimura N

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex.

【24h】

X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex.

机译：x射线和中子蛋白质晶体分析trypsin-BPTI复杂。

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

In this work, the crystal structure of the beta-trypsin-bovine pancreatic trypsin inhibitor (BPTI) complex was refined and the D and H atoms in the complex were identified using data from both 1.6 A resolution X-ray diffraction and 2.15 A resolution neutron diffraction. After crystallization in an H(2)O solution, the sample crystal was soaked in a D(2)O solution for about two weeks. The protonation states of the catalytic triad (Asp102, His57 and Ser195) were observed. These results confirmed that the nucleophilic reactivity of the hydroxyl group of Ser195 was increased by forming a hydrogen bond with His57. According to structural analysis, the trypsin-BPTI interfaces located at the scissile peptide and the active sites were inaccessible to solvent water, and the amide H atoms of P2' Arg17/I, Gly216/E and Gly193/E at the binding interface were protected from H/D exchange. In contrast, both the amide H atom of P1' Ala16/I of the scissile peptide bond P1-P1' and the H atom between His57 N(2) and Ser195 O(gamma) were replaced by D atoms. The hydrogen-bond networks at the S1 pocket were also confirmed and discussed from the viewpoint of substrate recognition. Moreover, the first neutron crystallographic structure of the Michaelis complex state of trypsin-BPTI is presented.

机译：在这部作品中,晶体的结构beta-trypsin-bovine胰腺胰蛋白酶抑制剂(BPTI)复杂精致,D和H原子使用数据在复杂中被确认x射线衍射分辨率1.6和2.15一项决议中子衍射。结晶在H (2) O解决方案中,示例水晶是浸泡在D (2) O的解决方案两个星期。催化三分子(Asp102 His57和Ser195)观察到。亲核活性的羟基Ser195增加了形成氢键His57。trypsin-BPTI接口位于易裂开的肽和活跃的网站都无法访问溶剂水和P2的酰胺H原子Arg17 /我,Gly216 / E和Gly193 / E的绑定从H / D交换接口被保护。相反,P1的酰胺H原子的Ala16 /我易裂开的肽键P1-P1”和H原子His57 N(2)之间和Ser195 O(γ)取而代之的是D原子。在S1口袋还证实,从底物的角度讨论识别。米歇利斯的晶体结构复杂trypsin-BPTI状态。

著录项

来源
《Acta crystallographica.Section D. Biological crystallography》 |2011年第2期|140-148|共9页
作者
Kawamura K; Yamada T; Kurihara KTamada TKuroki RTanaka ITakahashi HNiimura N;
展开▼
作者单位

Institute of Applied Beam Science, Graduate School of Science and Engineering, Ibaraki University, 4-12-1 Naka-Narusawa, Hitachi, Ibaraki 316-8511, Japan.;

展开▼
收录信息
原文格式 PDF
正文语种英语
中图分类化学;
关键词
Neutron diffraction; crystal structure; hydrogen bondsAtomsneutronsHydroxyl groupX-raysActive SiteCrystallizationamides;

机译：中子衍射;晶体结构;氢bondsAtomsneutronsHydroxyl groupX-raysActive;

相似文献

外文文献
中文文献

1. Neutronic analysis of ITER radial x-ray camera [J] . Luying NIU, Hongrui CAO, Kun XU, 等离子体科学和技术（英文版） . 2019,第002期
2. Optical 2-benzyl-5-hydroxy-4-oxopentanoic acids against carboxypeptidase A:Synthesis,kinetic evaluation and X-ray crystallographic study [J] . 无中国化学快报：英文版 . 2010,第002期
3. Data mining of Arabidopsis thaliana salt-response proteins based on bioinformatics analysis Guo Meili, Gao Weixi, Yu Xuejuan, Zhou Chunxi, Liu Fujun, Liu Xin Abstract [J] . Plant Omics . 2012,第1期

机译：Data mining of Arabidopsis thaliana salt-response proteins based on bioinformatics analysis Guo Meili, Gao Weixi, Yu Xuejuan, Zhou Chunxi, Liu Fujun, Liu Xin Abstract
4. Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein [O] . Chen I.J., Chou C.C., Liu C.L., 2014

机译：Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein

X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex.

摘要

著录项

相似文献

相关主题

期刊订阅