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pubmed-article:18930848pubmed:abstractTextSau3AI 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.lld:pubmed
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pubmed-article:18930848pubmed:authorpubmed-author:TangLinLlld:pubmed
pubmed-article:18930848pubmed:authorpubmed-author:ZhangZhi-Hong...lld:pubmed
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pubmed-article:18930848pubmed:year2009lld:pubmed
pubmed-article:18930848pubmed:articleTitleCrystal structure and function of C-terminal Sau3AI domain.lld:pubmed
pubmed-article:18930848pubmed:affiliationShanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China.lld:pubmed
pubmed-article:18930848pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18930848pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed