Crystal structures of the copper and nickel complexes of RNase A: Metal-induced interprotein interactions and identification of a novel copper binding motif

被引:21
作者
Balakrishnan, R
Ramasubbu, N
Varughese, KI
Parthasarathy, R
机构
[1] SUNY BUFFALO, DEPT ORAL BIOL, BUFFALO, NY 14214 USA
[2] ROSWELL PK CANC INST, DEPT BIOPHYS, BUFFALO, NY 14263 USA
[3] ROSWELL PK CANC INST, CTR CRYSTALLOG RES, BUFFALO, NY 14263 USA
[4] Scripps Res Inst, DEPT MOL & EXPT MED, LA JOLLA, CA 92037 USA
关键词
D O I
10.1073/pnas.94.18.9620
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
We report the crystal structures of the copper and nickel complexes of RNase A, The overall topology of these two complexes is similar to that of other RNase A structures, However, there are significant differences in the mode of binding of copper and nickel, There are two copper ions per molecule of the protein, but there is only one nickel ion per molecule of the protein, Significant changes occur in the interprotein interactions as a result of differences in the coordinating groups at the common binding site around Bis-105. Consequently, the copper-and nickel-ion-hound dimers of RNase A act as nucleation sites for generating different crystal lattices for the two complexes, A second copper ion is present at an active site residue His-119 for which all the ligands are from one molecule of the protein, At this second site, His-119 adopts an inactive conformation (B) induced by the copper. We have identified a novel copper binding motif involving the alpha-amino group and the N-terminal residues.
引用
收藏
页码:9620 / 9625
页数:6
相关论文
共 46 条
[1]   ENGINEERED METAL-BINDING PROTEINS - PURIFICATION TO PROTEIN FOLDING [J].
ARNOLD, FH ;
HAYMORE, BL .
SCIENCE, 1991, 252 (5014) :1796-1797
[2]   MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL-CHANGES INVOLVING ITS FUNCTIONAL SURFACE [J].
BELLSOLELL, L ;
PRIETO, J ;
SERRANO, L ;
COLL, M .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 238 (04) :489-495
[3]   NUCLEAR MAGNETIC-RESONANCE AND NEUTRON-DIFFRACTION STUDIES OF THE COMPLEX OF RIBONUCLEASE-A WITH URIDINE VANADATE, A TRANSITION-STATE ANALOG [J].
BORAH, B ;
CHEN, CW ;
EGAN, W ;
MILLER, M ;
WLODAWER, A ;
COHEN, JS .
BIOCHEMISTRY, 1985, 24 (08) :2058-2067
[4]   INCORPORATION OF A STABILIZING CA2+-BINDING LOOP INTO SUBTILISIN BPN' [J].
BRAXTON, S ;
WELLS, JA .
BIOCHEMISTRY, 1992, 31 (34) :7796-7801
[5]   METALLOTHIONEIN AND THE TRACE MINERALS [J].
BREMNER, I ;
BEATTIE, JH .
ANNUAL REVIEW OF NUTRITION, 1990, 10 :63-83
[6]   X-ray structures of a designed binding site in trypsin show metal-dependent geometry [J].
Brinen, LS ;
Willett, WS ;
Craik, CS ;
Fletterick, RJ .
BIOCHEMISTRY, 1996, 35 (19) :5999-6009
[7]  
BRUNGER AT, 1988, XPLOR MANUAL
[8]  
BUSH AI, 1994, J BIOL CHEM, V269, P12152
[9]   RAPID INDUCTION OF ALZHEIMER A-BETA AMYLOID FORMATION BY ZINC [J].
BUSH, AI ;
PETTINGELL, WH ;
MULTHAUP, G ;
PARADIS, MD ;
VONSATTEL, JP ;
GUSELLA, JF ;
BEYREUTHER, K ;
MASTERS, CL ;
TANZI, RE .
SCIENCE, 1994, 265 (5177) :1464-1467
[10]   INTERACTION OF METAL-IONS WITH CARBOXYLIC AND CARBOXAMIDE GROUPS IN PROTEIN STRUCTURES [J].
CHAKRABARTI, P .
PROTEIN ENGINEERING, 1990, 4 (01) :49-56