1u35: Difference between revisions
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|PDB= 1u35 |SIZE=350|CAPTION= <scene name='initialview01'>1u35</scene>, resolution 3.0Å | |PDB= 1u35 |SIZE=350|CAPTION= <scene name='initialview01'>1u35</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= H3FA, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= H3FA, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1aoi|1AOI]], [[1f66|1F66]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u35 OCA], [http://www.ebi.ac.uk/pdbsum/1u35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u35 RCSB]</span> | |||
}} | }} | ||
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[[Category: nucleosome]] | [[Category: nucleosome]] | ||
''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 00:04:47 2008'' | ||
Revision as of 00:04, 31 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | , , , | ||||||
| Gene: | H3FA, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL (Mus musculus) | ||||||
| Related: | 1AOI, 1F66
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
OverviewOverview
macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.
About this StructureAbout this Structure
1U35 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural characterization of the histone variant macroH2A., Chakravarthy S, Gundimella SK, Caron C, Perche PY, Pehrson JR, Khochbin S, Luger K, Mol Cell Biol. 2005 Sep;25(17):7616-24. PMID:16107708
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