1bh9: Difference between revisions
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|PDB= 1bh9 |SIZE=350|CAPTION= <scene name='initialview01'>1bh9</scene>, resolution 2.6Å | |PDB= 1bh9 |SIZE=350|CAPTION= <scene name='initialview01'>1bh9</scene>, resolution 2.6Å | ||
|SITE= <scene name='pdbsite=MRY:Binding+Site+Of+Hg+From+Pcmbs'>MRY</scene> | |SITE= <scene name='pdbsite=MRY:Binding+Site+Of+Hg+From+Pcmbs'>MRY</scene> | ||
|LIGAND= <scene name='pdbligand=PMB:PARA-MERCURY-BENZENESULFONIC ACID'>PMB</scene> | |LIGAND= <scene name='pdbligand=PMB:PARA-MERCURY-BENZENESULFONIC+ACID'>PMB</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh9 OCA], [http://www.ebi.ac.uk/pdbsum/1bh9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bh9 RCSB]</span> | |||
}} | }} | ||
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[[Category: Romier, C.]] | [[Category: Romier, C.]] | ||
[[Category: Ruff, M.]] | [[Category: Ruff, M.]] | ||
[[Category: histone fold]] | [[Category: histone fold]] | ||
[[Category: htafii18]] | [[Category: htafii18]] | ||
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[[Category: transcription regulation complex]] | [[Category: transcription regulation complex]] | ||
''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 19:01:00 2008'' | ||
Revision as of 19:01, 30 March 2008
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| , resolution 2.6Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS
OverviewOverview
Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions. The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed.
About this StructureAbout this Structure
1BH9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family., Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D, Cell. 1998 Jul 24;94(2):239-49. PMID:9695952
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