[English] 日本語
Yorodumi- SASDA56: BAZ2B in Tris (Bromodomain adjacent to zinc finger domain protein... -
+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDA56 |
---|---|
Sample | BAZ2B in Tris
|
Biological species | Homo sapiens (human) |
Citation | Journal: Structure / Year: 2015 Title: Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Authors: Cynthia Tallant / Erica Valentini / Oleg Fedorov / Lois Overvoorde / Fleur M Ferguson / Panagis Filippakopoulos / Dmitri I Svergun / Stefan Knapp / Alessio Ciulli / Abstract: Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA ...Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA by interactions with promoter-bound TTF-I, pRNA, and acetylation of H4K16. TIP5 domains that recognize posttranslational modifications on histones are essential for recruitment of NoRC to chromatin, but how these reader modules recognize site-specific histone tails has remained elusive. Here, we report crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones. PHD finger functions as an independent structural module in recognizing unmodified H3 histone tails, and the bromodomain prefers H3 and H4 acetylation marks followed by a key basic residue, KacXXR. Further low-resolution analyses of PHD-bromodomain modules provide molecular insights into their trans histone tail recognition, required for nucleosome recruitment and transcriptional repression of the NoRC complex. |
Contact author |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Models
Model #159 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
---|---|
Model #160 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
Model #161 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
Model #162 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
Model #163 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
Model #164 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
Model #165 | Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: BAZ2B in Tris / Specimen concentration: 10 mg/ml |
---|---|
Buffer | Name: Tris / Concentration: 20.00 mM / pH: 8 Composition: NaCl 500.000 mM, DTT 2.000 mM, ZnCl2 10.000 microM |
Entity #115 | Name: BAZ2B / Type: protein Description: Bromodomain adjacent to zinc finger domain protein 2B, C-terminal Formula weight: 27.67 / Num. of mol.: 1 / Source: Homo sapiens Sequence: AMASIMKVYC QICRKGDNEE LLLLCDGCDK GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKIKKLHV KGKKTNESKK GKKVTLTGDT EDEDSASTSS SLKRGNKDLK KRKMEENTSI NLSKQESFTS VKKPKRDDSK DLALCSMILT EMETHEDAWP FLLPVNLKLV ...Sequence: AMASIMKVYC QICRKGDNEE LLLLCDGCDK GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKIKKLHV KGKKTNESKK GKKVTLTGDT EDEDSASTSS SLKRGNKDLK KRKMEENTSI NLSKQESFTS VKKPKRDDSK DLALCSMILT EMETHEDAWP FLLPVNLKLV PGYKKVIKKP MDFSTIREKL SSGQYPNLET FALDVRLVFD NCETFNEDDS DIGRAGHNMR KYFEKKWTDT FKVS |
-Experimental information
Beam | Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Detector | Name: Pilatus 1M-W / Pixsize x: 0.172 mm | ||||||||||||||||||||||||||||||
Scan | Title: BAZ2B in Tris / Measurement date: Sep 24, 2012 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
| ||||||||||||||||||||||||||||||
Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 434 /
| ||||||||||||||||||||||||||||||
Result | Type of curve: single_conc /
|