pubmed-article:18930848 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:18930848 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
pubmed-article:18930848 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:18930848 | pubmed:dateCreated | 2008-11-28 | lld:pubmed |
pubmed-article:18930848 | pubmed:abstractText | Sau3AI 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 |
pubmed-article:18930848 | pubmed:language | eng | lld:pubmed |
pubmed-article:18930848 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18930848 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18930848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18930848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18930848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18930848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18930848 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18930848 | pubmed:month | Jan | lld:pubmed |
pubmed-article:18930848 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:DICKY PYP | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:FordF SFS | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:TangLinL | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:ZhangZhi-Hong... | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:SunLi-HuaLH | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:XuChun-YanCY | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:HeJian-HuaJH | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:XuSi-JieSJ | lld:pubmed |
pubmed-article:18930848 | pubmed:author | pubmed-author:HuXiao-JianXJ | lld:pubmed |
pubmed-article:18930848 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18930848 | pubmed:volume | 1794 | lld:pubmed |
pubmed-article:18930848 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18930848 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18930848 | pubmed:pagination | 118-23 | lld:pubmed |
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pubmed-article:18930848 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:18930848 | pubmed:articleTitle | Crystal structure and function of C-terminal Sau3AI domain. | lld:pubmed |
pubmed-article:18930848 | pubmed:affiliation | Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China. | lld:pubmed |
pubmed-article:18930848 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18930848 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |