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Structural and Functional Analysis of Validoxylamine A 7 '-phosphate Synthase ValL Involved in Validamycin A Biosynthesis

文献类型： 外文期刊

作者： Zheng, Lina 1 ; Zhou, Xiang 2 ; Zhang, Huaidong 1 ; Ji, Xiaofeng 4 ; Li, Lei 2 ; Huang, Lin 1 ; Bai, Linquan 2 ; Zhang, H 1 ;

作者机构： 1.Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Hubei, Peoples R China

2.Shanghai Jiao Tong Univ, State Key Lab Microbial Metab, Shanghai 200030, Peoples R China

3.Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, Shanghai 200030, Peoples R China

4.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qin

期刊名称：PLOS ONE （ 影响因子：3.24； 五年影响因子：3.788 ）

ISSN： 1932-6203

年卷期： 2012 年 7 卷 2 期

页码：

收录情况： SCI

摘要： Validamycin A (Val-A) is an effective antifungal agent widely used in Asian countries as crop protectant. Validoxylamine A, the core structure and intermediate of Val-A, consists of two C7-cyclitol units connected by a rare C-N bond. In the Val-A biosynthetic gene cluster in Streptomyces hygroscopicus 5008, the ORF valL was initially annotated as a validoxylamine A 7'-phosphate(V7P) synthase, whose encoded 497-aa protein shows high similarity with trehalose 6-phosphate(T6P) synthase. Gene inactivation of valL abolished both validoxylamine A and validamycin A productivity, and complementation with a cloned valL recovered 10% production of the wild-type in the mutant, indicating the involvement of ValL in validoxylamine A biosynthesis. Also we determined the structures of ValL and ValL/trehalose complex. The structural data indicates that ValL adopts the typical fold of GT-B protein family, featuring two Rossmann-fold domains and an active site at domain junction. The residues in the active site are arranged in a manner homologous to that of Escherichia coli (E. coli) T6P synthase OtsA. However, a significant discrepancy is found in the active-site loop region. Also noticeable structural variance is found around the active site entrance in the apo ValL structure while the region takes an ordered configuration upon binding of product analog trehalose. Furthermore, the modeling of V7P in the active site of ValL suggests that ValL might have a similar SNi-like mechanism as OtsA.

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