1cm0: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1cm0 |SIZE=350|CAPTION= <scene name='initialview01'>1cm0</scene>, resolution 2.3Å | |PDB= 1cm0 |SIZE=350|CAPTION= <scene name='initialview01'>1cm0</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene> | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cm0 OCA], [http://www.ebi.ac.uk/pdbsum/1cm0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cm0 RCSB]</span> | |||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Trievel, R C.]] | [[Category: Trievel, R C.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
[[Category: acetyltransferase]] | [[Category: acetyltransferase]] | ||
[[Category: coactivator]] | [[Category: coactivator]] | ||
| Line 34: | Line 36: | ||
[[Category: p300/cbp associated factor]] | [[Category: p300/cbp associated factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:18 2008'' | ||
Revision as of 19:24, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX
OverviewOverview
The human p300/CBP-associating factor, PCAF, mediates transcriptional activation through its ability to acetylate nucleosomal histone substrates as well as transcriptional activators such as p53. We have determined the 2.3 A crystal structure of the histone acetyltransferase (HAT) domain of PCAF bound to coenzyme A. The structure reveals a central protein core associated with coenzyme A binding and a pronounced cleft that sits over the protein core and is flanked on opposite sides by the N- and C-terminal protein segments. A correlation of the structure with the extensive mutagenesis data for PCAF and the homologous yeast GCN5 protein implicates the cleft and the N- and C-terminal protein segments as playing an important role in histone substrate binding, and a glutamate residue in the protein core as playing an essential catalytic role. A structural comparison with the coenzyme-bound forms of the related N-acetyltransferases, HAT1 (yeast histone acetyltransferase 1) and SmAAT (Serratia marcescens aminoglycoside 3-N-acetyltransferase), suggests the mode of substrate binding and catalysis by these enzymes and establishes a paradigm for understanding the structure-function relationships of other enzymes that acetylate histones and transcriptional regulators to promote activated transcription.
About this StructureAbout this Structure
1CM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A., Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R, EMBO J. 1999 Jul 1;18(13):3521-32. PMID:10393169
Page seeded by OCA on Sun Mar 30 19:24:18 2008