دورية أكاديمية
Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase.
| العنوان: | Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase. |
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| المؤلفون: | Wei Y; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville 22906-0011, USA., Contreras JA, Sheffield P, Osterlund T, Derewenda U, Kneusel RE, Matern U, Holm C, Derewenda ZS |
| المصدر: | Nature structural biology [Nat Struct Biol] 1999 Apr; Vol. 6 (4), pp. 340-5. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Nature Pub. Co Country of Publication: United States NLM ID: 9421566 Publication Model: Print Cited Medium: Print ISSN: 1072-8368 (Print) Linking ISSN: 10728368 NLM ISO Abbreviation: Nat Struct Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: New York, NY : Nature Pub. Co., c1994-c2003. |
| مواضيع طبية MeSH: | Bacillus subtilis/*enzymology , Bacterial Proteins/*chemistry , Carboxylic Ester Hydrolases/*chemistry , Carboxylic Ester Hydrolases/*genetics , Carboxylic Ester Hydrolases/*metabolism, Amino Acid Sequence ; Animals ; Bacillus subtilis/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Base Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Hormones/pharmacology ; Humans ; Mammals ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Reproducibility of Results ; Sequence Analysis/methods ; Sequence Homology, Amino Acid ; Sterol Esterase/drug effects ; Sterol Esterase/metabolism |
| مستخلص: | Brefeldin A esterase (BFAE), a detoxifying enzyme isolated from Bacillus subtilis, hydrolyzes and inactivates BFA, a potent fungal inhibitor of intracellular vesicle-dependent secretory transport and poliovirus RNA replication. We have solved the crystal structure of BFAE and we discovered that the previously reported amino acid sequence was in serious error due to frame shifts in the cDNA sequence. The correct sequence, inferred from the experimentally phased electron density map, revealed that BFAE is a homolog of the mammalian hormone sensitive lipase (HSL). It is a canonical alpha/beta hydrolase with two insertions forming the substrate binding pocket. The enzyme contains a lipase-like catalytic triad, Ser 202, Asp 308 and His 338, consistent with mutational studies that implicate the homologous Ser 424, Asp 693 and His 723 in the catalytic triad in human HSL. |
| سلسلة جزيئية: | GENBANK AF056081 PDB 1JKM |
| المشرفين على المادة: | 0 (Bacterial Proteins) 0 (Hormones) EC 3.1.1.- (Carboxylic Ester Hydrolases) EC 3.1.1.- (brefeldin A esterase) EC 3.1.1.13 (Sterol Esterase) |
| تواريخ الأحداث: | Date Created: 19990414 Date Completed: 19990423 Latest Revision: 20071115 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1038/7576 |
| PMID: | 10201402 |
| قاعدة البيانات: | MEDLINE |
Find this article in full text from Springer Verlag. | تدمد: | 1072-8368 |
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| DOI: | 10.1038/7576 |