CAS OpenIR  > 中科院上海应用物理研究所2011-2018年
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
Source PublicationJOURNAL OF BIOLOGICAL CHEMISTRY
ISSN0021-9258
Volume291Issue:30Pages:15575-15587
Subtype期刊论文
AbstractPyrroloquinoline 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
Indexed BySCI
Language英语
WOS IDWOS:000380584200014
Citation statistics
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/26461
Collection中科院上海应用物理研究所2011-2018年
Corresponding AuthorXu, DQ; Wang, WW (reprint author), Nanjing Agr Univ, Dept Microbiol, Coll Life Sci, Nanjing 210095, Jiangsu, Peoples R China.
Recommended Citation
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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