title: Topological chirality of iron-sulfur proteins.
abstract: An examination of x-ray structures of single-cluster [4Fe-4S] proteins in the Protein Data Bank has revealed that all redox proteins and the glutamine 5-phosphoribosyl-l-pyrophosphate amidotransferase from Bacillus subtilis have a topological configuration arbitrarily designated as D, whereas the DNA repair enzyme endonuclease III from Escherichia coli has the opposite topological configuration L. This is the first example in which both senses of topological chirality have been observed in a class of proteins.
authors.affiliation: Department of Chemistry, Princeton University, NJ 08544, USA.
authors.forename: C
authors.initials: C
authors.lastname: Liang
authors.forename: K
authors.initials: K
authors.lastname: Mislow
mesh_terms: D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure*; D010084:Oxidation-Reduction; D013237:Stereoisomerism
chemical_list: D007506:Iron-Sulfur Proteins