BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15944

Title: Structural Basis for the Regulation of p53 Function by p300   PubMed: 19217391

Authors: Bai, Yawen; Feng, Hanqiao; Jenkins, Lisa; Durell, Stewart; Wiodawer, Alex; Appella, Ettore

Citation: Feng, Hanqiao; Miller Jenkins, Lisa; Durell, Stewart; Hayashi, Ryo; Mazur, Sharlyn; Cherry, Scott; Tropea, Joseph; Miller, Maria; Wlodawer, Alexander; Appella, Ettore; Bai, Yawen. "Structural Basis for p300 Taz2-p53 TAD1 Binding and Modulation by Phosphorylation"  Structure 17, 202-210 (2009).

Assembly members:
TAZ2, polymer, 90 residues, 9963.838 Da.
TAD(1-39), polymer, 39 residues, 4351.815 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
TAZ2: ATQSPGDSRRLSIQRAIQSL VHAAQCRNANCSLPSCQKMK RVVQHTKGCKRKTNGGCPIC KQLIALAAYHAKHCQENKCP VPFCLNIKQK
TAD(1-39): MEEPQSDPSVEPPLSQETFS DLWKLLPENNVLSPLPSQA

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts111
1H chemical shifts751

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1TAZ21
2TAD(1-39)2

Entities:

Entity 1, TAZ2 90 residues - 9963.838 Da.

1-90 from p300(1723-1812)

1   ALATHRGLNSERPROGLYASPSERARGARG
2   LEUSERILEGLNARGALAILEGLNSERLEU
3   VALHISALAALAGLNCYSARGASNALAASN
4   CYSSERLEUPROSERCYSGLNLYSMETLYS
5   ARGVALVALGLNHISTHRLYSGLYCYSLYS
6   ARGLYSTHRASNGLYGLYCYSPROILECYS
7   LYSGLNLEUILEALALEUALAALATYRHIS
8   ALALYSHISCYSGLNGLUASNLYSCYSPRO
9   VALPROPHECYSLEUASNILELYSGLNLYS

Entity 2, TAD(1-39) 39 residues - 4351.815 Da.

1-39

1   METGLUGLUPROGLNSERASPPROSERVAL
2   GLUPROPROLEUSERGLNGLUTHRPHESER
3   ASPLEUTRPLYSLEULEUPROGLUASNASN
4   VALLEUSERPROLEUPROSERGLNALA

Samples:

p53cpx_3: TAZ2 1.1-1.2 mM; TAD(1-39), [U-100% 15N], 1.0-1.1 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM

TAZ2cpx_1: TAZ2, [U-100% 15N], 1.0-1.2 mM; TAD(1-39) 1.1-1.3 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM

TAZ2cpx_2: TAZ2, [U-100% 13C; U-100% 15N], 1.0-1.2 mM; TAD(1-39) 1.1-1.3 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM

TAZ2cpx_4: TAZ2 1.0-1.2 mM; TAD(1-39) 1.1-1.3 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.3; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCTAZ2cpx_1isotropicsample_conditions_1
2D 1H-1H NOESYTAZ2cpx_4isotropicsample_conditions_1
3D CBCA(CO)NHTAZ2cpx_2isotropicsample_conditions_1
3D HNCACBTAZ2cpx_2isotropicsample_conditions_1
3D HNCOTAZ2cpx_2isotropicsample_conditions_1
3D HN(CA)COTAZ2cpx_2isotropicsample_conditions_1
3D HNCATAZ2cpx_2isotropicsample_conditions_1
3D H(CCO)NHTAZ2cpx_2isotropicsample_conditions_1
3D HCCH-TOCSYTAZ2cpx_2isotropicsample_conditions_1
3D HNHATAZ2cpx_1isotropicsample_conditions_1
3D 1H-15N NOESYTAZ2cpx_1isotropicsample_conditions_1
3D 1H-13C NOESYTAZ2cpx_2isotropicsample_conditions_1
2D 1H-15N HSQCp53cpx_3isotropicsample_conditions_1
3D CBCA(CO)NHp53cpx_3isotropicsample_conditions_1
3D HNCACBp53cpx_3isotropicsample_conditions_1
3D HNCAp53cpx_3isotropicsample_conditions_1
3D HNCOp53cpx_3isotropicsample_conditions_1
3D HN(CA)COp53cpx_3isotropicsample_conditions_1
3D H(CCO)NHp53cpx_3isotropicsample_conditions_1
3D HCCH-TOCSYp53cpx_3isotropicsample_conditions_1
3D 1H-15N NOESYp53cpx_3isotropicsample_conditions_1
3D 1H-13C NOESYp53cpx_3isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe vupdated, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView vupdated, Johnson, One Moon Scientific - chemical shift assignment

X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TALOS vupdated, Cornilescu, Delaglio and Bax - structure solution

ProcheckNMR vupdated, Laskowski and MacArthur - structure validation

MolProbity v3.15, Richardson - structure validation

InsightII vupdated, Accelrys Software Inc. - figure preparation

SYBYL v8.0, Tripos - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker DRX 700 MHz

Related Database Links:

BMRB 25484 17073 17760 18709
PDB
DBJ BAC16799 BAG35463 BAG59884 BAG60244 BAI45431
EMBL CAA26306 CAA34420 CAA38095 CAA42625 CAA42626
GB AAA17994 AAA59987 AAA59988 AAA59989 AAA61211
PRF 2006287A
REF NP_000537 NP_001040616 NP_001119584 NP_001119585 NP_001119586
SP P04637 P13481 P56423 P56424 P61260