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2bfq
From Proteopedia
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|PDB= 2bfq |SIZE=350|CAPTION= <scene name='initialview01'>2bfq</scene>, resolution 1.5Å | |PDB= 2bfq |SIZE=350|CAPTION= <scene name='initialview01'>2bfq</scene>, resolution 1.5Å | ||
|SITE= <scene name='pdbsite=AC1:Apr+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Apr+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene> | + | |LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfq OCA], [http://www.ebi.ac.uk/pdbsum/2bfq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bfq RCSB]</span> | ||
}} | }} | ||
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[[Category: Pugieux, C.]] | [[Category: Pugieux, C.]] | ||
[[Category: Sait, F.]] | [[Category: Sait, F.]] | ||
| - | [[Category: APR]] | ||
[[Category: crystal structure p-loop]] | [[Category: crystal structure p-loop]] | ||
[[Category: histone macroh2a]] | [[Category: histone macroh2a]] | ||
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[[Category: nucleotide]] | [[Category: nucleotide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:05:44 2008'' |
Revision as of 23:05, 30 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES
Overview
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.
About this Structure
2BFQ is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
The macro domain is an ADP-ribose binding module., Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG, EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274
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