Title of article :
The Crystal Structure of AF1521 a Protein from Archaeoglobus fulgidus with Homology to the Non-histone Domain of MacroH2A
Author/Authors :
Mark D. Allen، نويسنده , , Ashley M. Buckle، نويسنده , , Suzanne C. Cordell، نويسنده , , Jan L?we، نويسنده , , Mark Bycroft، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2003
Pages :
9
From page :
503
To page :
511
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 1.7 Å of AF1521, a protein consisting of a stand-alone macro domain from Archaeoglobus fulgidus. The structure has a mixed α/β 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.
Keywords :
histone macroH2A , crystal structure , RNA binding , X-chromosome inactivation , P-loop nucleotide hydrolases
Journal title :
Journal of Molecular Biology
Serial Year :
2003
Journal title :
Journal of Molecular Biology
Record number :
1242794
Link To Document :
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