| pubmed-article:11106757 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
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| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1414639 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1333931 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1548174 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C1706076 | lld:lifeskim |
| pubmed-article:11106757 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:11106757 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11106757 | pubmed:dateCreated | 2002-1-7 | lld:pubmed |
| pubmed-article:11106757 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:abstractText | Esa1 is the catalytic subunit of the NuA4 histone acetylase (HAT) complex that acetylates histone H4, and it is a member of the MYST family of HAT proteins that includes the MOZ oncoprotein and the HIV-1 Tat interacting protein Tip60. Here we report the X-ray crystal structure of the HAT domain of Esa1 bound to coenzyme A and investigate the protein's catalytic mechanism. Our data reveal that Esa1 contains a central core domain harboring a putative catalytic base, and flanking domains that are implicated in histone binding. Comparisons with the Gcn5/PCAF and Hat1 proteins suggest a unified mechanism of catalysis and histone binding by HAT proteins, whereby a structurally conserved core domain mediates catalysis, and sequence variability within a structurally related N- and C-terminal scaffold determines substrate specificity. | lld:pubmed |
| pubmed-article:11106757 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11106757 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106757 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11106757 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11106757 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:11106757 | pubmed:author | pubmed-author:BergerS LSL | lld:pubmed |
| pubmed-article:11106757 | pubmed:author | pubmed-author:YanYY | lld:pubmed |
| pubmed-article:11106757 | pubmed:author | pubmed-author:BarlevN ANA | lld:pubmed |
| pubmed-article:11106757 | pubmed:author | pubmed-author:MarmorsteinRR | lld:pubmed |
| pubmed-article:11106757 | pubmed:author | pubmed-author:HannaT ATA | lld:pubmed |
| pubmed-article:11106757 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11106757 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:11106757 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11106757 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11106757 | pubmed:pagination | 1195-205 | lld:pubmed |
| pubmed-article:11106757 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11106757 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11106757 | pubmed:articleTitle | Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases. | lld:pubmed |
| pubmed-article:11106757 | pubmed:affiliation | The Wistar Institute University of Pennsylvania, Philadelphia, PA 19104, USA. | lld:pubmed |
| pubmed-article:11106757 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11106757 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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