| pubmed-article:7664065 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C0036765 | lld:lifeskim |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C0014230 | lld:lifeskim |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C0311474 | lld:lifeskim |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:7664065 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:7664065 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:7664065 | pubmed:dateCreated | 1995-10-10 | lld:pubmed |
| pubmed-article:7664065 | pubmed:abstractText | The crystal structure of Serratia endonuclease has been solved to 2.1 A by multiple isomorphous replacement. This magnesium-dependent enzyme is equally active against single- and double-stranded DNA, as well as RNA, without any apparent base preference. The Serratia endonuclease fold is distinct from that of other nucleases that have been solved by X-ray diffraction. The refined structure consists of a central layer containing six antiparallel beta-strands which is flanked on one side by a helical domain and on the opposite side by one dominant helix and a very long coiled loop. Electrostatic calculations reveal a strongly polarized molecular surface and suggest that a cleft between this long helix and loop, near His 89, may contain the active site of the enzyme. | lld:pubmed |
| pubmed-article:7664065 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7664065 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7664065 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7664065 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7664065 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7664065 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:7664065 | pubmed:author | pubmed-author:MillerM DMD | lld:pubmed |
| pubmed-article:7664065 | pubmed:author | pubmed-author:TannerJJ | lld:pubmed |
| pubmed-article:7664065 | pubmed:author | pubmed-author:AlpaughMM | lld:pubmed |
| pubmed-article:7664065 | pubmed:author | pubmed-author:BenedikM JMJ | lld:pubmed |
| pubmed-article:7664065 | pubmed:author | pubmed-author:KrauseK LKL | lld:pubmed |
| pubmed-article:7664065 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7664065 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:7664065 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7664065 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7664065 | pubmed:pagination | 461-8 | lld:pubmed |
| pubmed-article:7664065 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:7664065 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7664065 | pubmed:articleTitle | 2.1 A structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA. | lld:pubmed |
| pubmed-article:7664065 | pubmed:affiliation | Department of Biochemical and Biophysical Sciences, University of Houston, Texas 77204-5934, USA. | lld:pubmed |
| pubmed-article:7664065 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7664065 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7664065 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7664065 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| family:PF01223.18 | family:pubmed | pubmed-article:7664065 | lld:pfam |
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