Ontology highlight
ABSTRACT:
SUBMITTER: Gold B
PROVIDER: S-EPMC2749609 | biostudies-literature | 2008 Oct
REPOSITORIES: biostudies-literature
Gold Ben B Deng Haiteng H Bryk Ruslana R Vargas Diana D Eliezer David D Roberts Julia J Jiang Xiuju X Nathan Carl C
Nature chemical biology 20080824 10
A screen of a genomic library from Mycobacterium tuberculosis (Mtb) identified a small, unannotated open reading frame (MT0196) that encodes a 4.9-kDa, cysteine-rich protein. Despite extensive nucleotide divergence, the amino acid sequence is highly conserved among mycobacteria that are pathogenic in vertebrate hosts. We synthesized the protein and found that it preferentially binds up to six Cu(I) ions in a solvent-shielded core. Copper, cadmium and compounds that generate nitric oxide or super ...[more]