کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2187727 1096136 2008 12 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
High-resolution Structure of ybfF from Escherichia coli K12: A Unique Substrate-binding Crevice Generated by Domain Arrangement
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
High-resolution Structure of ybfF from Escherichia coli K12: A Unique Substrate-binding Crevice Generated by Domain Arrangement
چکیده انگلیسی

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 Å, respectively. The structure of Ec_ybfF is composed of a globular α/β hydrolase domain with a three-helical bundle cap, which is linked by a kinked helix to the α/β 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 α/β 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 α/β 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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 376, Issue 5, 7 March 2008, Pages 1426–1437
نویسندگان
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