Crystal structure and function of C-terminal Sau3AI domain
文献类型：期刊论文
| 作者 | Xu, CY（徐春艳） ; Yu, F（郁峰） ; Xu, SJ（许世杰） ; Ding, Y ; Sun, LH ; Tang, L（唐琳） ; Hu, XJ ; Zhang, ZH ; He, JH（何建华） |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2009 |
| 卷号 | 1794期号:1页码:118 |
| ISSN号 | 1570-9639 |
| 通讯作者 | Hu, XJ (reprint author), Fudan Univ, Dept Phys & Biophys, Shanghai 200433, Peoples R China |
| 英文摘要 | Sau3AI is a type 11 restriction enzyme that recognizes the 5'-GATC-3' sequence in double-strand DNA and cleaves at 5' to the G residue. The C-terminal domain of SaU3AI (Sau3AI-C), which contains amino acids from 233 to 489, was crystallized and its structure was solved by using the Multi-wavelength Anomalous Diffraction method. The Sau3AI-C structure at 1.9 angstrom resolution is similar to the structure of MutH, a DNA mismatch repair protein that shares high sequence similarity with the N-terminal Sau3AI domain. The functional analysis shows that Sau3AI-C can bind DNA with one recognition sequence but has no cleavage activity. These results indicate that Sau3AI is a pseudo-dimer belonging to the type IIe restriction enzymes and the Sau3AI-C is the allosteric effector domain that assists DNA binding and cleavage. (C) 2008 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000261863300014 |
| 公开日期 | 2012-04-18 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/7680]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2004-2010年 |
| 推荐引用方式 GB/T 7714 | Xu, CY,Yu, F,Xu, SJ,et al. Crystal structure and function of C-terminal Sau3AI domain[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2009,1794(1):118. |
| APA | Xu, CY.,Yu, F.,Xu, SJ.,Ding, Y.,Sun, LH.,...&He, JH.(2009).Crystal structure and function of C-terminal Sau3AI domain.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1794(1),118. |
| MLA | Xu, CY,et al."Crystal structure and function of C-terminal Sau3AI domain".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1794.1(2009):118. |
入库方式： OAI收割
来源：上海应用物理研究所
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