1HJZ

Crystal structure of AF1521 protein containing a macroH2A domain

Summary for 1HJZ

• Entry DOI: 10.2210/pdb1hjz/pdb
• Descriptor: HYPOTHETICAL PROTEIN AF1521, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: macro_h2a domain/hydrolase, histone macroh2a, crystal structure p-loop nucleotide hydrolase, macro_h2a domain-hydrolase complex
• Biological source: ARCHAEOGLOBUS FULGIDUS
• Total number of polymer chains: 2
• Total formula weight: 42356.95

Authors

Allen, M.D.,Buckle, A.M.,Cordell, S.C.,Lowe, J.,Bycroft, M. (deposition date: 2003-03-05, release date: 2003-07-10, Last modification date: 2024-11-20)

Primary citation

Allen, M.D.,Buckle, A.M.,Cordell, S.C.,Lowe, J.,Bycroft, M.
The Crystal Structure of Af1521 a Protein from Archaeoglobus Fulgidus with Homology to the Non-Histone Domain of Macroh2A
J.Mol.Biol., 330:503-, 2003

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.

PubMed: 12842467
DOI: 10.1016/S0022-2836(03)00473-X

Experimental method

X-RAY DIFFRACTION (1.7 Å)