2BFR

The Macro domain is an ADP-ribose binding module

Summary for 2BFR

• Entry DOI: 10.2210/pdb2bfr/pdb
• Related: 1HJZ 1VHU 2BFQ
• Descriptor: HYPOTHETICAL PROTEIN AF1521, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: histone macroh2a, crystal structure p-loop, nucleotide, hydrolase, macro_h2a domain/hydrolase, macro_h2a domain-hydrolase complex
• Biological source: ARCHAEOGLOBUS FULGIDUS
• Total number of polymer chains: 1
• Total formula weight: 21462.75

Authors

Karras, G.I.,Buhecha, H.R.,Allen, M.D.,Pugieux, C.,Sait, F.,Bycroft, M.,Ladurner, A.G. (deposition date: 2004-12-10, release date: 2004-12-16, Last modification date: 2024-11-20)

Primary citation

Karras, G.I.,Kustatscher, G.,Buhecha, H.R.,Allen, M.D.,Pugieux, C.,Sait, F.,Bycroft, M.,Ladurner, A.G.
The Macro Domain is an Adp-Ribose Binding Module.
Embo J., 24:1911-, 2005

PubMed Abstract: The ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose.

PubMed: 15902274
DOI: 10.1038/SJ.EMBOJ.7600664

Experimental method

X-RAY DIFFRACTION (2.5 Å)