AMINO-ACID-SEQUENCE AND PREDICTED 3-DIMENSIONAL STRUCTURE OF PEA SEED (PISUM-SATIVUM) FERRITIN

被引:80
作者
LOBREAUX, S
YEWDALL, SJ
BRIAT, JF
HARRISON, PM
机构
[1] LAB BIOL MOLEC VEGETALE, CNRS, URA 1178, BP 53X, F-38041 GRENOBLE, FRANCE
[2] UNIV SHEFFIELD, KREBS INST BIOMOLEC RES, DEPT MOLEC BIOL & BIOTECHNOL, SHEFFIELD S10 2UH, ENGLAND
[3] UNIV JOSEPH FOURIER, F-38041 GRENOBLE, FRANCE
基金
英国惠康基金;
关键词
D O I
10.1042/bj2880931
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The iron storage protein, ferritin, is widely distributed in the living kingdom. Here the complete cDNA and derived amino-acid sequence of pea seed ferritin are described, together with its predicted secondary structure, namely a four-helix-bundle fold similar to those of mammalian ferritins, with a fifth short helix at the C-terminus. An N-terminal extension of 71 residues contains a transit peptide (first 47 residues) responsible for plastid targetting as in other plant ferritins, and this is cleaved before assembly. The second part of the extension (24 residues) belongs to the mature subunit; it is cleaved during germination. The amino-acid sequence of pea seed ferritin is aligned with those of other ferritins (49% amino-acid identity with H-chains and 40% with L-chains of human liver ferritin in the aligned region). A three-dimensional model has been constructed by fitting the aligned sequence to the coordinates of human H-chains, with appropriate modifications. A folded conformation with an 11-residue helix is predicted for the N-terminal extension. As in mammalian ferritins, 24 subunits assemble into a hollow shell. In pea seed ferritin, its N-terminal extension is exposed on the outside surface of the shell. Within each pea subunit is a ferroxidase centre resembling those of human ferritin H-chains except for a replacement of Glu-62 by His. The channel at the 4-fold-symmetry axes defined by E-helices, is predicted to be hydrophilic in plant ferritins, whereas it is hydrophobic in mammalian ferritins.
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页码:931 / 939
页数:9
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