The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A.
MacroH2A is an unusual histone H2A variant that has an extensive C-terminal tail that comprises approximately two thirds of the protein. The C-terminal non-histone domain of macroH2A is also found in a number of other proteins and has been termed the macro domain. Here we report the crystal structure to 1.7A of AF1521, a protein consisting of a stand-alone macro domain from Archaeoglobus fulgidus. The structure has a mixed alpha/beta fold that closely resembles the N-terminal DNA binding domain of the Escherichia coli leucine aminopeptidase PepA. The structure also shows some similarity to members of the P-loop family of nucleotide hydrolases.
Allen
Mark D
MD
MRC Centre for Protein Engineering, and Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Buckle
Ashley M
AM
Cordell
Suzanne C
SC
Löwe
Jan
J
Bycroft
Mark
M
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D019611:Archaeoglobus fulgidus / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D004303:Dosage Compensation, Genetic; D006657:Histones / Q000737:chemistry*; D006867:Hydrolases / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D006657:Histones; C120756:macroH2A histone; C111749:pseudomonas exoprotein A protein, Pseudomonas aeruginosa; D012313:RNA; D004247:DNA; D006867:Hydrolases