2bfr: Difference between revisions
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|PDB= 2bfr |SIZE=350|CAPTION= <scene name='initialview01'>2bfr</scene>, resolution 2.5Å | |PDB= 2bfr |SIZE=350|CAPTION= <scene name='initialview01'>2bfr</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfr OCA], [http://www.ebi.ac.uk/pdbsum/2bfr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bfr RCSB]</span> | |||
}} | }} | ||
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[[Category: Pugieux, C.]] | [[Category: Pugieux, C.]] | ||
[[Category: Sait, F.]] | [[Category: Sait, F.]] | ||
[[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 02:05:48 2008'' | ||
Revision as of 02:05, 31 March 2008
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| , resolution 2.5Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE
OverviewOverview
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 StructureAbout this Structure
2BFR is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
ReferenceReference
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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