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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2000-2-3
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pubmed:abstractText |
Homing endonucleases are classified into four families based on active site sequence motifs. Through structural comparisons we have found structural similarities between the endonuclease domain of colicin E9, an H-N-H motif-containing enzyme, and both the non-specific nuclease from Serratia and I-PpoI, a His-Cys box-containing homing endonuclease. Our comparison identifies conservation at the heart of all three enzyme active sites and so argues for a re-classification of H-N-H and His-Cys box homing endonucleases as a single family. We suggest the 'betabetaalpha-Me family' of homing enzymes to reflect the three elements of secondary structure and the metal ion that define the motif.
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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 |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
463
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-2
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:10601625-Amino Acids,
pubmed-meshheading:10601625-Bacterial Proteins,
pubmed-meshheading:10601625-Binding Sites,
pubmed-meshheading:10601625-Colicins,
pubmed-meshheading:10601625-Conserved Sequence,
pubmed-meshheading:10601625-Endodeoxyribonucleases,
pubmed-meshheading:10601625-Endonucleases,
pubmed-meshheading:10601625-Models, Molecular,
pubmed-meshheading:10601625-Protein Conformation,
pubmed-meshheading:10601625-Protein Structure, Secondary
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pubmed:year |
1999
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pubmed:articleTitle |
Structural parsimony in endonuclease active sites: should the number of homing endonuclease families be redefined?
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pubmed:affiliation |
School of Chemical Sciences, University of East Anglia, Norwich, UK.
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pubmed:publicationType |
Journal Article
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