The Crystal Structure of Af1521 a Protein from Archaeoglobus Fulgidus with Homology to the Non-Histone Domain of Macroh2A
Allen, M.D., Buckle, A.M., Cordell, S.C., Lowe, J., Bycroft, M.(2003) J Mol Biol 330: 503
- PubMed: 12842467 
- DOI: https://doi.org/10.1016/s0022-2836(03)00473-x
- Primary Citation of Related Structures:  
1HJZ - PubMed Abstract: 
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.
Organizational Affiliation: 
MRC Centre for Protein Engineering, and Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.