The structure of the metal-binding motif GMTCAAC is similar in an 18-residue linear peptide and the mercury binding protein MerP

被引:53
作者
Veglia, G [1 ]
Porcelli, F [1 ]
DeSilva, T [1 ]
Prantner, A [1 ]
Opella, SJ [1 ]
机构
[1] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA
关键词
D O I
10.1021/ja992908z
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
引用
收藏
页码:2389 / 2390
页数:2
相关论文
共 31 条
[1]   HG-199 NMR INVESTIGATION ON THE SOLUTION STRUCTURE OF HG(II) COMPLEXES OF OLIGOPEPTIDES CONTAINING CYSTEINE AND HISTIDINE-RESIDUES [J].
ADACHI, H ;
UEYAMA, N ;
NAKAMURA, A .
INORGANICA CHIMICA ACTA, 1992, 198 :805-811
[2]  
BERTINI I, 1995, SPECIFIC FACTORS MET, V1, P81
[3]   BACTERIAL-RESISTANCE TO MERCURY - REDUCTIO AD ABSURDUM [J].
BROWN, NL .
TRENDS IN BIOCHEMICAL SCIENCES, 1985, 10 (10) :400-403
[4]  
BRUNGER AT, 1992, XPLOR VERSION 3 1 SY
[5]   THE WILSON DISEASE GENE IS A PUTATIVE COPPER TRANSPORTING P-TYPE ATPASE SIMILAR TO THE MENKES GENE [J].
BULL, PC ;
THOMAS, GR ;
ROMMENS, JM ;
FORBES, JR ;
COX, DW .
NATURE GENETICS, 1993, 5 (04) :327-337
[6]   A MER-LUX TRANSCRIPTIONAL FUSION FOR REAL-TIME EXAMINATION OF INVIVO GENE-EXPRESSION KINETICS AND PROMOTER RESPONSE TO ALTERED SUPERHELICITY [J].
CONDEE, CW ;
SUMMERS, AO .
JOURNAL OF BACTERIOLOGY, 1992, 174 (24) :8094-8101
[7]   The copper chaperone for superoxide dismutase [J].
Culotta, VC ;
Klomp, LWJ ;
Strain, J ;
Casareno, RLB ;
Krems, B ;
Gitlin, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (38) :23469-23472
[8]  
da Silva JJR Frausto., 1991, BIOL CHEM ELEMENTS
[9]   MOLECULAR CHARACTERIZATION OF A COPPER TRANSPORT PROTEIN IN SACCHAROMYCES-CEREVISIAE - AN UNEXPECTED ROLE FOR COPPER IN IRON TRANSPORT [J].
DANCIS, A ;
YUAN, DS ;
HAILE, D ;
ASKWITH, C ;
EIDE, D ;
MOEHLE, C ;
KAPLAN, J ;
KLAUSNER, RD .
CELL, 1994, 76 (02) :393-402
[10]   Optimizing the metal binding parameters of an EF-hand-like calcium chelation loop: Coordinating side chains play a more important tuning role than chelation loop flexibility [J].
Drake, SK ;
Zimmer, MA ;
Miller, CL ;
Falke, JJ .
BIOCHEMISTRY, 1997, 36 (32) :9917-9926