| pubmed-article:9482715 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9482715 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9482715 | lifeskim:mentions | umls-concept:C0007292 | lld:lifeskim |
| pubmed-article:9482715 | lifeskim:mentions | umls-concept:C0008855 | lld:lifeskim |
| pubmed-article:9482715 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:9482715 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:9482715 | lifeskim:mentions | umls-concept:C0003737 | lld:lifeskim |
| pubmed-article:9482715 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9482715 | pubmed:dateCreated | 1998-4-16 | lld:pubmed |
| pubmed-article:9482715 | pubmed:abstractText | In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein (ACP) synthases catalyze chain elongation by the addition of two-carbon units derived from malonyl-ACP to an acyl group bound to either ACP or CoA. The crystal structure of beta-ketoacyl synthase II from Escherichia coli has been determined with the multiple isomorphous replacement method and refined at 2.4 A resolution. The subunit consists of two mixed five-stranded beta-sheets surrounded by alpha-helices. The two sheets are packed against each other in such a way that the fold can be described as consisting of five layers, alpha-beta-alpha-beta-alpha. The enzyme is a homodimer, and the subunits are related by a crystallographic 2-fold axis. The two active sites are located near the dimer interface but are approximately 25 A apart. The proposed nucleophile in the reaction, Cys163, is located at the bottom of a mainly hydrophobic pocket which is also lined with several conserved polar residues. In spite of very low overall sequence homology, the structure of beta-ketoacyl synthase is similar to that of thiolase, an enzyme involved in the beta-oxidation pathway, indicating that both enzymes might have a common ancestor. | lld:pubmed |
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| pubmed-article:9482715 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9482715 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9482715 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9482715 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9482715 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9482715 | pubmed:author | pubmed-author:SchneiderGG | lld:pubmed |
| pubmed-article:9482715 | pubmed:author | pubmed-author:HuangWW | lld:pubmed |
| pubmed-article:9482715 | pubmed:author | pubmed-author:EdwardsPP | lld:pubmed |
| pubmed-article:9482715 | pubmed:author | pubmed-author:LindqvistYY | lld:pubmed |
| pubmed-article:9482715 | pubmed:author | pubmed-author:JiaJJ | lld:pubmed |
| pubmed-article:9482715 | pubmed:author | pubmed-author:DeheshKK | lld:pubmed |
| pubmed-article:9482715 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9482715 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:9482715 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:9482715 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9482715 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9482715 | pubmed:pagination | 1183-91 | lld:pubmed |
| pubmed-article:9482715 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:9482715 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9482715 | pubmed:articleTitle | Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. | lld:pubmed |
| pubmed-article:9482715 | pubmed:affiliation | Division of Structural Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:9482715 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9482715 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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