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

TY - JOUR

T1 - Crystal structures of the copper and nickel complexes of rnase A

T2 - Metal-induced interprotein interactions and identification of a novel copper binding motif

AU - Balakrislman, R.

AU - Ramasubbu, N.

AU - Vanmhese, K. I.

AU - Parthasartln, R.

PY - 1997

Y1 - 1997

N2 - We report the cnslal structures of the copper and nickel complexes of RNasc A The overall lopolog) of these complexes is similar to that of oilier RNase A structures Ho\\c\er. there arc significant differences in the inudc of binding ol copper and nickel There arc tv\o copper ions per molecule of the protein, uhiic there is only one nickel ion per molecule of the protein. Significant changes occur in the interprotcin interactions as a result of differences in the coordinating groups at the common binding site around His-105. Consequently, the copper and nickel ion-bound dimers of RNasc A act as nuclcation sites for generating different cnstal lattices for the two complexes A second copper ion is present at an active site residue, His-119 for which all the hgands arc from one molecule of the protein Al this second site. His-11'J adopts an inactive conformation (B) induced b> the copper ion Thus, copper mimics the role of an inhibitor for RNasc A We have identified a no\cl copper binding motif based on the structure of the RNase-Cu complex in comparison with the cnstal structures of GK-GK-GK and the copper complex of ThiorcdoMii This motif consists of the a-ammo gioup and the backbone electron donois of the N-lcrmmal residues A mechanism for metal induced aggregation in the case of some amyloid diseases has been proposed based on these studies.

AB - We report the cnslal structures of the copper and nickel complexes of RNasc A The overall lopolog) of these complexes is similar to that of oilier RNase A structures Ho\\c\er. there arc significant differences in the inudc of binding ol copper and nickel There arc tv\o copper ions per molecule of the protein, uhiic there is only one nickel ion per molecule of the protein. Significant changes occur in the interprotcin interactions as a result of differences in the coordinating groups at the common binding site around His-105. Consequently, the copper and nickel ion-bound dimers of RNasc A act as nuclcation sites for generating different cnstal lattices for the two complexes A second copper ion is present at an active site residue, His-119 for which all the hgands arc from one molecule of the protein Al this second site. His-11'J adopts an inactive conformation (B) induced b> the copper ion Thus, copper mimics the role of an inhibitor for RNasc A We have identified a no\cl copper binding motif based on the structure of the RNase-Cu complex in comparison with the cnstal structures of GK-GK-GK and the copper complex of ThiorcdoMii This motif consists of the a-ammo gioup and the backbone electron donois of the N-lcrmmal residues A mechanism for metal induced aggregation in the case of some amyloid diseases has been proposed based on these studies.

UR - https://www.scopus.com/pages/publications/33750104894

UR - https://www.scopus.com/inward/citedby.url?scp=33750104894&partnerID=8YFLogxK

M3 - Article

SN - 0892-6638

VL - 11

SP - A909

JO - FASEB Journal

JF - FASEB Journal

IS - 9

ER -