2reu
Crystal Structure of the C-terminal of Sau3AI fragmentCrystal Structure of the C-terminal of Sau3AI fragment
Structural highlights
Function[T2S3_STAAU] Recognizes the double-stranded sequence GATC and cleaves before G-1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSau3AI is a type II 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 A 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. Crystal structure and function of C-terminal Sau3AI domain.,Xu CY, Yu F, Xu SJ, Ding Y, Sun LH, Tang L, Hu XJ, Zhang ZH, He JH Biochim Biophys Acta. 2009 Jan;1794(1):118-23. doi: 10.1016/j.bbapap.2008.09.008., Epub 2008 Oct 1. PMID:18930848[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||