The Crystal Structure of N10-Formyltetrahydrofolate Synthetase from Moorella thermoacetica

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• 作者：Ramin Radfar ; Ronald Shin ; George M. Sheldrick ; Wladek Minor ; Charles R. Lovell ; Jerome D. Odom ; R. Bruce Dunlap ; and Lukasz Lebioda
• 刊名：Biochemistry
• 出版年：2000
• 出版时间：April 11, 2000
• 年：2000
• 卷：39
• 期：14
• 页码：3920 - 3926
• 全文大小：784K
• 年卷期：v.39,no.14(April 11, 2000)
• ISSN：1520-4995

文摘

The structure was solved at 2.5 Å resolution using multiwavelength anomalous dispersion(MAD) scattering by Se-Met residues. The subunit of N¹⁰-formyltetrahydrofolate synthetase is composedof three domains organized around three mixed mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheets. There are two cavities between adjacent domains.One of them was identified as the nucleotide binding site by homology modeling. The large domaincontains a seven-stranded mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheet surrounded by helices on both sides. The second domain contains afive-stranded mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheet with two mages/gifchars/alpha.gif" BORDER=0>-helices packed on one side while the other two are a wall of the activesite cavity. The third domain contains a four-stranded mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheet forming a half-barrel. The concave side iscovered by two helices while the convex side is another wall of the large cavity. Arg 97 is likely involvedin formyl phosphate binding. The tetrameric molecule is relatively flat with the shape of the letter X, andthe active sites are located at the end of the subunits far from the subunit interface.