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| pubmed-article:8171031 | lifeskim:mentions | umls-concept:C0051581 | lld:lifeskim |
| pubmed-article:8171031 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:8171031 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8171031 | lifeskim:mentions | umls-concept:C0039219 | lld:lifeskim |
| pubmed-article:8171031 | lifeskim:mentions | umls-concept:C0052908 | lld:lifeskim |
| pubmed-article:8171031 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8171031 | pubmed:dateCreated | 1994-6-1 | lld:pubmed |
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| pubmed-article:8171031 | 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. | lld:pubmed |
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| pubmed-article:8171031 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8171031 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8171031 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8171031 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8171031 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8171031 | pubmed:author | pubmed-author:StudierF WFW | lld:pubmed |
| pubmed-article:8171031 | pubmed:author | pubmed-author:PflugrathJ... | lld:pubmed |
| pubmed-article:8171031 | pubmed:author | pubmed-author:ZhangXX | lld:pubmed |
| pubmed-article:8171031 | pubmed:author | pubmed-author:ChengXX | lld:pubmed |
| pubmed-article:8171031 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8171031 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:8171031 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:8171031 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8171031 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8171031 | pubmed:pagination | 4034-8 | lld:pubmed |
| pubmed-article:8171031 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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| pubmed-article:8171031 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8171031 | pubmed:articleTitle | The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. | lld:pubmed |
| pubmed-article:8171031 | pubmed:affiliation | W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, NY 11724. | lld:pubmed |
| pubmed-article:8171031 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8171031 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8171031 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8171031 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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