Stereochemistry of guanidine-metal interactions: Implications for L-arginine-metal interactions in protein structure and function
| Autor: | David W. Christianson, Luigi Di Costanzo, Lloyd V. Flores |
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| Přispěvatelé: | Di Costanzo, L., Flores, Jr. L. V., Christianson, D. W. |
| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Metalloenzyme Metal-ligand coordination Molecular Conformation Stereoisomerism Biotin synthase Arginine Biochemistry Structure-Activity Relationship chemistry.chemical_compound Protein structure Structural Biology Metals Heavy Humans Moiety Binding site Guanidine Molecular Biology Binding Sites biology Chemistry Hydrogen bond Crystal structure Protein Binding Site Proteins Hydrogen Bonding computer.file_format Protein Data Bank Amino acid biology.protein computer Human |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 65:637-642 |
| ISSN: | 1097-0134 0887-3585 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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