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Solution structure of PAFP-S: A new knottin-type antifungal peptide from the seeds of Phytolacca americana
Gao, GH; Liu, W; Dai, JX; Wang, JF; Hu, Z; Zhang, Y; Wang, DC
2001-09-18
Source PublicationBIOCHEMISTRY
ISSN0006-2960
Volume40Issue:37Pages:10973-10978
AbstractThe three-dimensional solution structure of PAFP-S, an antifungal peptide extracted from the seeds of Phytolacca americana, was determined using H-1 NMR spectroscopy. This cationic peptide contains 38 amino acid residues. Its structure was determined from 302 distance restraints and 36 dihedral restraints derived from NOEs and coupling constants. The peptide has six cysteines involved in three disulfide bonds. The previously unassigned parings have now been determined from NMR data. The solution structure of PAFP-S is presented as a set of 20 structures using ab initio dynamic simulated annealing, with an average RMS deviation of 1.68 Angstrom for the backbone heavy atoms and 2.19 Angstrom for all heavy atoms, respectively. For the well-defined triple-stranded beta -sheet involving residues 8-10, 23-27, and 32-36, the corresponding values were 0.39 and 1.25 Angstrom. The global fold involves a cystine-knotted three-stranded antiparallel beta -sheet (residues 8-10, 23-27, 32-36), a flexible loop (residues 14-19), and four beta -reverse turns (residues 4-8, 11-14, 19-22, 28-32). This structure features all the characteristics of the knottin fold. It is the first structural model of an antifungal peptide that adopts a knottin-type structure. PAFP-S has an extended hydrophobic surface comprised of residues Tyr23, Phe25, Ile27, Tyr32, and Val34. The side chains of these residues are well-defined in the NMR structure. Several hydrophilic and positively charged residues (Arg9, Arg38, and Lys36) surround the hydrophobic surface, giving PAFP-S an amphiphilic character which would be the main structural basis of its biological function.
Subject AreaBiochemistry & Molecular Biology
DOI10.1021/bi010167k
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000171032400007
Citation statistics
Cited Times:29[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.kib.ac.cn/handle/151853/14189
Collection离退休
Affiliation1.Chinese Acad Sci, Inst Biophys, Natl Lab Macromol, Lab Mol Biophys, Beijing 100101, Peoples R China
2.Chinese Acad Sci, Kunming Inst Bot, Kunming 650204, Peoples R China
Recommended Citation
GB/T 7714
Gao, GH,Liu, W,Dai, JX,et al. Solution structure of PAFP-S: A new knottin-type antifungal peptide from the seeds of Phytolacca americana[J]. BIOCHEMISTRY,2001,40(37):10973-10978.
APA Gao, GH.,Liu, W.,Dai, JX.,Wang, JF.,Hu, Z.,...&Wang, DC.(2001).Solution structure of PAFP-S: A new knottin-type antifungal peptide from the seeds of Phytolacca americana.BIOCHEMISTRY,40(37),10973-10978.
MLA Gao, GH,et al."Solution structure of PAFP-S: A new knottin-type antifungal peptide from the seeds of Phytolacca americana".BIOCHEMISTRY 40.37(2001):10973-10978.
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