The geometries of 150 guanidine-metal ion interactions retrieved from crystal structures deposited in the Cambridge Structural Database have been analyzed. Metal ions exhibit a preference for anti coordination stereochemistry in the plane of the unprotonated guanidine group, usually in chelate complexes with a diguanidine moiety, but syn-oriented interactions are occasionally found for single guanidine-metal interactions. Three L-arginine-metal coordination interactions are found in metalloenzyme structures deposited in the Protein Data Bank: biotin synthase from E. coli, His-67 → Arg human carbonic anhydrase I, and inactivated B. caldovelox arginase complexed with L-arginine. In these proteins, L-arginine-metal coordination adopts syn/out-of-plane and anti/in-plane coordination stereochemistry. The implications of these results for L-arginine-metal interactions in protein structure and function are discussed. Although such interactions are rare, this analysis serves as a useful reference point for the growing interest in enzymes containing L-arginine residues that function as general bases or metal ligands. © 2006 Wiley-Liss, Inc.

Stereochemistry of guanidine-metal interactions: Implications for L-arginine-metal interactions in protein structure and function

Di Costanzo L.
Primo
Conceptualization
;
2006

Abstract

The geometries of 150 guanidine-metal ion interactions retrieved from crystal structures deposited in the Cambridge Structural Database have been analyzed. Metal ions exhibit a preference for anti coordination stereochemistry in the plane of the unprotonated guanidine group, usually in chelate complexes with a diguanidine moiety, but syn-oriented interactions are occasionally found for single guanidine-metal interactions. Three L-arginine-metal coordination interactions are found in metalloenzyme structures deposited in the Protein Data Bank: biotin synthase from E. coli, His-67 → Arg human carbonic anhydrase I, and inactivated B. caldovelox arginase complexed with L-arginine. In these proteins, L-arginine-metal coordination adopts syn/out-of-plane and anti/in-plane coordination stereochemistry. The implications of these results for L-arginine-metal interactions in protein structure and function are discussed. Although such interactions are rare, this analysis serves as a useful reference point for the growing interest in enzymes containing L-arginine residues that function as general bases or metal ligands. © 2006 Wiley-Liss, Inc.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/899745
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