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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1994-6-1
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pubmed:databankReference |
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pubmed:abstractText |
The lysozyme of bacteriophage T7 is a bifunctional protein that cuts amide bonds in the bacterial cell wall and binds to and inhibits transcription by T7 RNA polymerase. The structure of a mutant T7 lysozyme has been determined by x-ray crystallography and refined at 2.2-A resolution. The protein folds into an alpha/beta-sheet structure that has a prominent cleft. A zinc atom is located in the cleft, bound directly to three amino acids and, through a water molecule, to a fourth. Zinc is required for amidase activity but not for inhibition of T7 RNA polymerase. Alignment of the zinc ligands of T7 lysozyme with those of carboxypeptidase A and thermolysin suggests structural similarity among the catalytic sites for the amidase and these zinc proteases. Mutational analysis identified presumed catalytic residues for amidase activity within the cleft and a surface that appears to be the site of binding to T7 RNA polymerase. Binding of T7 RNA polymerase inhibits amidase activity.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-1099209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-17810339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-2023259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-2104979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-2199796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-273244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-3568126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-4554613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-4582731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-4902069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-4934313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-6864790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-7277500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8171031-7688864
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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 |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4034-8
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:8171031-Amidohydrolases,
pubmed-meshheading:8171031-Amino Acid Sequence,
pubmed-meshheading:8171031-Bacteriophage T7,
pubmed-meshheading:8171031-Binding Sites,
pubmed-meshheading:8171031-Crystallography, X-Ray,
pubmed-meshheading:8171031-DNA-Directed RNA Polymerases,
pubmed-meshheading:8171031-Metalloproteins,
pubmed-meshheading:8171031-Molecular Sequence Data,
pubmed-meshheading:8171031-Muramidase,
pubmed-meshheading:8171031-Protein Structure, Tertiary,
pubmed-meshheading:8171031-Structure-Activity Relationship,
pubmed-meshheading:8171031-Viral Proteins,
pubmed-meshheading:8171031-Zinc
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pubmed:year |
1994
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pubmed:articleTitle |
The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase.
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pubmed:affiliation |
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, NY 11724.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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