| pubmed-article:19706470 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19706470 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:19706470 | lifeskim:mentions | umls-concept:C0033618 | lld:lifeskim |
| pubmed-article:19706470 | lifeskim:mentions | umls-concept:C1412587 | lld:lifeskim |
| pubmed-article:19706470 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19706470 | lifeskim:mentions | umls-concept:C1705938 | lld:lifeskim |
| pubmed-article:19706470 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:19706470 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:19706470 | pubmed:dateCreated | 2009-10-6 | lld:pubmed |
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| pubmed-article:19706470 | pubmed:abstractText | The Get3 ATPase directs the delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (ER). TA-proteins are characterized by having a single transmembrane helix (TM) at their extreme C terminus and include many essential proteins, such as SNAREs, apoptosis factors, and protein translocation components. These proteins cannot follow the SRP-dependent co-translational pathway that typifies most integral membrane proteins; instead, post-translationally, these proteins are recognized and bound by Get3 then delivered to the ER in the ATP dependent Get pathway. To elucidate a molecular mechanism for TA protein binding by Get3 we have determined three crystal structures in apo and ADP forms from Saccharomyces cerevisae (ScGet3-apo) and Aspergillus fumigatus (AfGet3-apo and AfGet3-ADP). Using structural information, we generated mutants to confirm important interfaces and essential residues. These results point to a model of how Get3 couples ATP hydrolysis to the binding and release of TA-proteins. | lld:pubmed |
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| pubmed-article:19706470 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19706470 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19706470 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19706470 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19706470 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:19706470 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:19706470 | pubmed:author | pubmed-author:ClemonsWillia... | lld:pubmed |
| pubmed-article:19706470 | pubmed:author | pubmed-author:SulowayChrist... | lld:pubmed |
| pubmed-article:19706470 | pubmed:author | pubmed-author:ChartronJusti... | lld:pubmed |
| pubmed-article:19706470 | pubmed:author | pubmed-author:ZaslaverMa'ay... | lld:pubmed |
| pubmed-article:19706470 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19706470 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:19706470 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:19706470 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19706470 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19706470 | pubmed:pagination | 14849-54 | lld:pubmed |
| pubmed-article:19706470 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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| pubmed-article:19706470 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19706470 | pubmed:articleTitle | Model for eukaryotic tail-anchored protein binding based on the structure of Get3. | lld:pubmed |
| pubmed-article:19706470 | pubmed:affiliation | Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA. | lld:pubmed |
| pubmed-article:19706470 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19706470 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19706470 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19706470 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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