| pubmed-article:18215690 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C0596533 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:18215690 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:18215690 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18215690 | pubmed:dateCreated | 2008-2-18 | lld:pubmed |
| pubmed-article:18215690 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18215690 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18215690 | pubmed:abstractText | Esterases are one of the most common enzymes and are involved in diverse cellular functions. ybfF protein from Escherichia coli (Ec_ybfF) belongs to the esterase family for the large substrates, palmitoyl coenzyme A and malonyl coenzyme A, which are important cellular intermediates for energy conversion and biomolecular synthesis. To obtain molecular information on ybfF esterase, which is found in a wide range of microorganisms, we elucidated the crystal structures of Ec_ybfF in complexes with small molecules at resolutions of 1.1 and 1.68 A, respectively. The structure of Ec_ybfF is composed of a globular alpha/beta hydrolase domain with a three-helical bundle cap, which is linked by a kinked helix to the alpha/beta hydrolase domain. It contains a catalytic tetrad of Ser-His-Asp-Ser with the first Ser acting as a nucleophile. The unique spatial arrangement and orientation of the helical cap with respect to the alpha/beta hydrolase domain form a substrate-binding crevice for large substrates. The helical cap is also directly involved in catalysis by providing a substrate anchor, viz., the conserved residues of Arg123 and Tyr208. The high-resolution structure of Ec_ybfF shows that the inserted helical bundle structure and its spatial orientation with respect to the alpha/beta hydrolase domain are critical for creating a large inner space and constituting a specific active site, thereby providing the broad substrate spectrum toward large biomolecules. | lld:pubmed |
| pubmed-article:18215690 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18215690 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18215690 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18215690 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18215690 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18215690 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18215690 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18215690 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18215690 | pubmed:issn | 1089-8638 | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:JungChe-HunCH | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:KimYong-SungY... | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:KimJeong-SunJ... | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:LeeSang-HakSH | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:NishiKosukeK | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:LeeJieunJ | lld:pubmed |
| pubmed-article:18215690 | pubmed:author | pubmed-author:ParkSuk-YoulS... | lld:pubmed |
| pubmed-article:18215690 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18215690 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:18215690 | pubmed:volume | 376 | lld:pubmed |
| pubmed-article:18215690 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18215690 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18215690 | pubmed:pagination | 1426-37 | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:meshHeading | pubmed-meshheading:18215690... | lld:pubmed |
| pubmed-article:18215690 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18215690 | pubmed:articleTitle | High-resolution structure of ybfF from Escherichia coli K12: a unique substrate-binding crevice generated by domain arrangement. | lld:pubmed |
| pubmed-article:18215690 | pubmed:affiliation | Department of Chemistry and Institute of Basic Sciences, Chonnam National University, 300 Yongbong-dong, Buk-gu, Gwangju 500-757, Korea. | lld:pubmed |
| pubmed-article:18215690 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18215690 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:945288 | entrezgene:pubmed | pubmed-article:18215690 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18215690 | lld:entrezgene |
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