Homology modeling of the multicopper oxidase Fet3 gives new insights in the mechanism of iron transport in yeast

被引:22
作者
di Patti, MCB
Pascarella, S
Catalucci, D
Calabrese, L
机构
[1] Univ Rome La Sapienza, Dipartimento Sci Biochim A Rossi Fanelli, I-00185 Rome, Italy
[2] Univ Rome La Sapienza, CNR, Ctr Biol Mol, I-00185 Rome, Italy
[3] Terza Univ Roma, Dipartimento Biol, I-00146 Rome, Italy
来源
PROTEIN ENGINEERING | 1999年 / 12卷 / 11期
关键词
cupredoxin; ferroxidase activity; Fet3; homology modeling;
D O I
10.1093/protein/12.11.895
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
Fet3, the multicopper oxidase of yeast, oxidizes extracellular ferrous iron which is then transported into the cell through the permease Ftr1, A three-dimensional model structure of Fet3 has been derived by homology modeling, Fet3 consists of three cupredoxin domains joined by a trinuclear copper cluster which is connected to the blue copper site located in the third domain. Close to this site, which is the primary electron acceptor from the substrate, residues for a potential iron binding site could be identified. The surface disposition of negatively charged residues suggests that Fet3 can translocate Fe3+ to the permease Ftr1 through a pathway under electrostatic guidance.
引用
收藏
页码:895 / 897
页数:3
相关论文
共 16 条
[1]   Iron and copper transport in yeast and its relevance to human disease [J].
Askwith, C ;
Kaplan, J .
TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (04) :135-138
[2]   Site-directed mutagenesis of the yeast multicopper oxidase Fet3p [J].
Askwith, CC ;
Kaplan, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (35) :22415-22419
[3]   THE FET3 GENE-PRODUCT REQUIRED FOR HIGH-AFFINITY IRON TRANSPORT IN YEAST IS A CELL-SURFACE FERROXIDASE [J].
DESILVA, DM ;
ASKWITH, CC ;
EIDE, D ;
KAPLAN, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (03) :1098-1101
[4]   An extensively modified version of MolScript that includes greatly enhanced coloring capabilities [J].
Esnouf, RM .
JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 1997, 15 (02) :132-+
[5]   CLUSTAL - A PACKAGE FOR PERFORMING MULTIPLE SEQUENCE ALIGNMENT ON A MICROCOMPUTER [J].
HIGGINS, DG ;
SHARP, PM .
GENE, 1988, 73 (01) :237-244
[6]   PROCHECK - A PROGRAM TO CHECK THE STEREOCHEMICAL QUALITY OF PROTEIN STRUCTURES [J].
LASKOWSKI, RA ;
MACARTHUR, MW ;
MOSS, DS ;
THORNTON, JM .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1993, 26 :283-291
[7]   An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity [J].
Lindley, PF ;
Card, G ;
Zaitseva, I ;
Zaitsev, V ;
Reinhammar, B ;
SelinLindgren, E ;
Yoshida, K .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 1997, 2 (04) :454-463
[8]   ASSESSMENT OF PROTEIN MODELS WITH 3-DIMENSIONAL PROFILES [J].
LUTHY, R ;
BOWIE, JU ;
EISENBERG, D .
NATURE, 1992, 356 (6364) :83-85
[9]   THE BLUE OXIDASES, ASCORBATE OXIDASE, LACCASE AND CERULOPLASMIN - MODELING AND STRUCTURAL RELATIONSHIPS [J].
MESSERSCHMIDT, A ;
HUBER, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1990, 187 (02) :341-352
[10]   REFINED CRYSTAL-STRUCTURE OF ASCORBATE OXIDASE AT 1.9 A RESOLUTION [J].
MESSERSCHMIDT, A ;
LADENSTEIN, R ;
HUBER, R ;
BOLOGNESI, M ;
AVIGLIANO, L ;
PETRUZZELLI, R ;
ROSSI, A ;
FINAZZIAGRO, A .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 224 (01) :179-205