2reu
Crystal Structure of the C-terminal of Sau3AI fragmentCrystal Structure of the C-terminal of Sau3AI fragment
Structural highlights
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
|
| ||||||||||||||||||||