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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1995-10-10
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
461-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7664065-Amino Acid Sequence,
pubmed-meshheading:7664065-Binding Sites,
pubmed-meshheading:7664065-Chemistry, Physical,
pubmed-meshheading:7664065-Crystallography, X-Ray,
pubmed-meshheading:7664065-DNA, Bacterial,
pubmed-meshheading:7664065-Endodeoxyribonucleases,
pubmed-meshheading:7664065-Endoribonucleases,
pubmed-meshheading:7664065-Magnesium,
pubmed-meshheading:7664065-Models, Chemical,
pubmed-meshheading:7664065-Models, Molecular,
pubmed-meshheading:7664065-Molecular Sequence Data,
pubmed-meshheading:7664065-Nucleic Acid Conformation,
pubmed-meshheading:7664065-Physicochemical Phenomena,
pubmed-meshheading:7664065-Protein Binding,
pubmed-meshheading:7664065-Protein Conformation,
pubmed-meshheading:7664065-Protein Structure, Tertiary,
pubmed-meshheading:7664065-Serratia marcescens
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pubmed:year |
1994
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pubmed:articleTitle |
2.1 A structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA.
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pubmed:affiliation |
Department of Biochemical and Biophysical Sciences, University of Houston, Texas 77204-5934, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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