Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway
Wei, QE; Ran, TT; Ma, CC; He, JH; Xu, DQ; Wang, WW; Wang, WW (reprint author), Nanjing Agr Univ, Dept Microbiol, Coll Life Sci, Nanjing 210095, Jiangsu, Peoples R China.
2016
发表期刊JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN0021-9258
卷号291期号:30页码:15575-15587
文章类型期刊论文
摘要Pyrroloquinoline quinone (PQQ) has received considerable attention due to its numerous important physiological functions. PqqA is a precursor peptide of PQQ with two conserved residues: glutamate and tyrosine. After linkage of the C gamma of glutamate and C epsilon of tyrosine by PqqE, these two residues are hypothesized to be cleaved from PqqA by PqqF. The linked glutamate and tyrosine residues are then used to synthesize PQQ. Here, we demonstrated that the pqqF gene is essential for PQQ biosynthesis as deletion of it eliminated the inhibition of prodigiosin production by glucose. We further determined the crystal structure of PqqF, which has a closed clamshell-like shape. The PqqF consists of two halves composed of an N-and a C-terminal lobe. The PqqF-N and PqqF-C lobes form a chamber with the volume of the cavity of similar to 9400 angstrom(3). The PqqF structure conforms to the general structure of inverzincins. Compared with the most thoroughly characterized inverzincin insulin-degrading enzyme, the size of PqqF chamber is markedly smaller, which may define the specificity for its substrate PqqA. Furthermore, the 14-amino acid-residue-long tag formed by the N-terminal tag from expression vector precisely protrudes into the counterpart active site; this N-terminal tag occupies the active site and stabilizes the closed, inactive conformation. His-48, His-52, Glu-129 and His-14 from the N-terminal tag coordinate with the zinc ion. Glu-51 acts as a base catalyst. The observed histidine residue-mediated inhibition may be applicable for the design of a peptide for the inhibition of M16 metalloproteases.
DOI10.1074/jbc.M115.711226
收录类别SCI
语种英语
WOS记录号WOS:000380584200014
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文献类型期刊论文
条目标识符http://ir.sinap.ac.cn/handle/331007/26461
专题中科院上海应用物理研究所2011-2018年
通讯作者Xu, DQ; Wang, WW (reprint author), Nanjing Agr Univ, Dept Microbiol, Coll Life Sci, Nanjing 210095, Jiangsu, Peoples R China.
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GB/T 7714
Wei, QE,Ran, TT,Ma, CC,et al. Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(30):15575-15587.
APA Wei, QE.,Ran, TT.,Ma, CC.,He, JH.,Xu, DQ.,...&Wang, WW .(2016).Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway.JOURNAL OF BIOLOGICAL CHEMISTRY,291(30),15575-15587.
MLA Wei, QE,et al."Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway".JOURNAL OF BIOLOGICAL CHEMISTRY 291.30(2016):15575-15587.
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