[English] 日本語
Yorodumi
- PDB-3i59: Crystal structure of MtbCRP in complex with N6-cAMP -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3i59
TitleCrystal structure of MtbCRP in complex with N6-cAMP
Components(Transcriptional regulator, Crp/Fnr ...Transcriptional regulation) x 2
KeywordsDNA BINDING PROTEIN / Mycobacterium Tuberculosis / cAMP Receptor Protein / CRP / allosteric mechanism / DNA binding / inhibition / N6-cAMP / Structural Genomics / TB Structural Genomics Consortium / TBSGC / DNA-binding / Transcription / Transcription regulation
Function / homology
Function and homology information


cell wall / cAMP binding / peptidoglycan-based cell wall / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / DNA binding / plasma membrane / cytosol
Similarity search - Function
helix_turn_helix, cAMP Regulatory protein / Crp-type HTH domain profile. / Crp-like helix-turn-helix domain / Crp-type HTH domain / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / Jelly Rolls ...helix_turn_helix, cAMP Regulatory protein / Crp-type HTH domain profile. / Crp-like helix-turn-helix domain / Crp-type HTH domain / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / Jelly Rolls / RmlC-like jelly roll fold / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Jelly Rolls / Winged helix-like DNA-binding domain superfamily / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Chem-N6R / Chem-N6S / CRP-like cAMP-activated global transcriptional regulator / CRP-like cAMP-activated global transcriptional regulator
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.29 Å
AuthorsReddy, M.C. / Palaninathan, S.K. / Bruning, J.B. / Thurman, C. / Smith, D. / Sacchettini, J.C. / TB Structural Genomics Consortium (TBSGC)
CitationJournal: J.Biol.Chem. / Year: 2009
Title: Structural Insights into the Mechanism of the Allosteric Transitions of Mycobacterium tuberculosis cAMP Receptor Protein.
Authors: Reddy, M.C. / Palaninathan, S.K. / Bruning, J.B. / Thurman, C. / Smith, D. / Sacchettini, J.C.
History
DepositionJul 3, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software
Revision 1.3Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif / struct_site
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 22, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Transcriptional regulator, Crp/Fnr family
B: Transcriptional regulator, Crp/Fnr family
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,1725
Polymers55,2412
Non-polymers9303
Water1,65792
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2840 Å2
ΔGint-15.3 kcal/mol
Surface area20000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)113.732, 75.716, 63.639
Angle α, β, γ (deg.)90.000, 110.910, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-270-

HOH

-
Components

-
Transcriptional regulator, Crp/Fnr ... , 2 types, 2 molecules AB

#1: Protein Transcriptional regulator, Crp/Fnr family / Transcriptional regulation


Mass: 27644.188 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: MT3777, Rv3676 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O69644, UniProt: P9WMH3*PLUS
#2: Protein Transcriptional regulator, Crp/Fnr family / Transcriptional regulation


Mass: 27597.293 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: MT3777, Rv3676 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O69644, UniProt: P9WMH3*PLUS

-
Non-polymers , 4 types, 95 molecules

#3: Chemical ChemComp-N6R / (2R)-N6-(1-Methyl-2-phenylethyl)adenosine-3',5'-cyclic monophosphate / (2R,4aS,6R,7R,7aR)-6-(6-{[(1R)-1-methyl-2-phenylethyl]amino}-9H-purin-9-yl)tetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinine-2,7-diol 2-oxide


Mass: 447.382 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H22N5O6P
#4: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-N6S / (2S)-N6-(1-Methyl-2-phenylethyl)adenosine-3',5'-cyclic monophosphate / (2S,4aS,6R,7R,7aR)-6-(6-{[(1S)-1-methyl-2-phenylethyl]amino}-9H-purin-9-yl)tetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphi nine-2,7-diol 2-oxide


Mass: 447.382 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H22N5O6P
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 92 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.32 Å3/Da / Density % sol: 46.91 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 2 microliters of protein + 2 microliters of well solution. Well solution was 0.4M NaH2PO4/1.6M K2HPO4, 0.1M Imidazole pH 8.0, 0.2M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.9791 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 10, 2008
Details: Mirrors: Adjustable focus K-B pair Si plus Pt, Rh coatings
RadiationMonochromator: Si(111) Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 2.29→20 Å / Num. all: 22400 / Num. obs: 22400 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 55.032 Å2 / Rmerge(I) obs: 0.058 / Rsym value: 0.058 / Χ2: 1.275 / Net I/σ(I): 15.1
Reflection shellResolution: 2.29→2.38 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.419 / Mean I/σ(I) obs: 2.6 / Num. unique all: 2028 / Rsym value: 0.419 / Χ2: 1.038 / % possible all: 89

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3I54
Resolution: 2.29→19.477 Å / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.741 / Isotropic thermal model: TLS / σ(F): 0 / σ(I): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.284 1149 5.13 %Random
Rwork0.234 ---
all0.234 22393 --
obs0.234 22393 98.35 %-
Solvent computationBsol: 56.737 Å2 / ksol: 0.285 e/Å3
Displacement parametersBiso max: 174.44 Å2 / Biso mean: 72.976 Å2 / Biso min: 29.75 Å2
Baniso -1Baniso -2Baniso -3
1--1.701 Å20 Å20.338 Å2
2--1.511 Å20 Å2
3---0.19 Å2
Refinement stepCycle: LAST / Resolution: 2.29→19.477 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3095 0 63 92 3250
Refine LS restraints
Refine-IDTypeDev idealWeight
X-RAY DIFFRACTIONf_angle_d0.8021
X-RAY DIFFRACTIONf_bond_d0.0061
X-RAY DIFFRACTIONf_chiral_restr0.0561
X-RAY DIFFRACTIONf_dihedral_angle_d11.8481
X-RAY DIFFRACTIONf_plane_restr0.0031
X-RAY DIFFRACTIONf_nbd_refined4.0671
LS refinement shell
Resolution (Å)Rfactor RworkNum. reflection RworkRefine-IDNum. reflection obsTotal num. of bins used% reflection obs (%)
2.29-2.3090.338430X-RAY DIFFRACTION4304279
2.309-2.3280.315462X-RAY DIFFRACTION4289
2.328-2.3480.32495X-RAY DIFFRACTION4290
2.348-2.3680.301515X-RAY DIFFRACTION4292
2.368-2.3890.326453X-RAY DIFFRACTION4292
2.389-2.4110.293526X-RAY DIFFRACTION4294
2.411-2.4340.33516X-RAY DIFFRACTION4296
2.434-2.4570.301526X-RAY DIFFRACTION4295
2.457-2.4820.274473X-RAY DIFFRACTION4292
2.482-2.5070.277497X-RAY DIFFRACTION4293
2.507-2.5340.276567X-RAY DIFFRACTION4297
2.534-2.5620.283479X-RAY DIFFRACTION4296
2.562-2.5910.29516X-RAY DIFFRACTION4295
2.591-2.6210.287509X-RAY DIFFRACTION4296
2.621-2.6530.264536X-RAY DIFFRACTION4296
2.653-2.6870.264487X-RAY DIFFRACTION4294
2.687-2.7220.318515X-RAY DIFFRACTION4294
2.722-2.7590.285506X-RAY DIFFRACTION4294
2.759-2.7980.277534X-RAY DIFFRACTION4296
2.798-2.840.272493X-RAY DIFFRACTION4296
2.84-2.8840.273536X-RAY DIFFRACTION4296
2.884-2.9310.292489X-RAY DIFFRACTION4295
2.931-2.9820.287531X-RAY DIFFRACTION4295
2.982-3.0360.266516X-RAY DIFFRACTION4296
3.036-3.0940.271514X-RAY DIFFRACTION4295
3.094-3.1570.242523X-RAY DIFFRACTION4296
3.157-3.2250.248505X-RAY DIFFRACTION4295
3.225-3.30.276508X-RAY DIFFRACTION4294
3.3-3.3820.245513X-RAY DIFFRACTION4295
3.382-3.4730.24505X-RAY DIFFRACTION4296
3.473-3.5740.223544X-RAY DIFFRACTION4296
3.574-3.6890.222506X-RAY DIFFRACTION4295
3.689-3.820.216518X-RAY DIFFRACTION4295
3.82-3.9710.218523X-RAY DIFFRACTION4294
3.971-4.150.18498X-RAY DIFFRACTION4294
4.15-4.3660.179513X-RAY DIFFRACTION4295
4.366-4.6360.161512X-RAY DIFFRACTION4293
4.636-4.9880.201508X-RAY DIFFRACTION4293
4.988-5.4790.215518X-RAY DIFFRACTION4294
5.479-6.2470.245529X-RAY DIFFRACTION4296
6.247-7.7790.224517X-RAY DIFFRACTION4293
7.779-18.9610.209383X-RAY DIFFRACTION4267
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.51261.5505-6.47025.6058-5.31282.07840.0541-0.57530.5108-0.2676-0.796-1.0721-0.38731.83390.75750.65040.11950.16420.69430.28210.59263.024111.9152-50.7918
2-0.2656-0.5975-4.32540.15032.42492.87380.48690.88460.58750.94580.17280.72440.570.7579-0.71560.98120.4360.16241.5236-0.07521.0914-0.23294.6379-52.185
32.6062-1.29590.31132.3603-0.22912.52070.0110.14920.4429-0.0456-0.1659-0.16850.0239-0.52060.10520.52860.06290.01540.41560.06210.499-10.858421.1113-45.2351
43.7271.64160.15154.26393.09113.0965-0.24560.27080.033-0.51730.6133-0.2071-0.27290.7216-0.19190.3921-0.07710.05240.37280.0360.3545-0.853112.0441-36.2982
57.19760.818-0.94799.3790.90354.05281.5635-0.96530.7272-0.6337-0.7775-0.4798-1.30510.3206-0.28420.6455-0.1946-0.04910.63010.02471.92582.997940.7917-34.221
61.69853.67071.6732-0.8105-3.2763.0368-0.11610.47460.81440.2043-0.09610.4062-0.41240.370.28830.50430.0479-0.00410.49450.29791.15533.57238.4108-45.9601
70.59232.85910.42083.93655.66122.13030.1840.393-0.07881.1255-0.3920.29763.1838-0.5839-0.03591.2697-0.03690.02250.6580.10840.8451-12.3805-0.2951-18.9136
85.2991-0.2081-0.63780.82320.38835.2796-1.0854-0.5463-0.58260.11840.46390.43440.27051.26070.49930.66670.05910.04360.53330.10070.6943-1.0818-1.927-12.3173
90.6570.0243-1.13561.1781-0.1011.4569-0.03370.3133-0.08720.0933-0.076-0.16920.00360.330.07320.3634-0.049-0.0270.52870.00810.35831.073313.9807-17.094
102.17231.16640.97522.92531.31644.69370.3730.2441-0.4280.14410.1932-0.608-0.38540.5969-0.60140.37770.1542-0.04180.563-0.08310.45640.0997-0.3123-22.5469
111.2559-0.15010.96392.93880.14491.00060.0746-0.09170.12940.81940.23360.23830.1258-0.6223-0.22630.47220.00430.02320.5516-0.01680.3931-9.132712.9565-29.617
123.093-1.1317-0.46023.7766-0.8231.8107-0.16720.15530.22750.22990.35220.3663-0.3561-0.1134-0.14830.52760.01880.01040.48470.10450.4916-16.558427.1116-11.0905
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 0:12)A0 - 12
2X-RAY DIFFRACTION2(chain A and resid 13:27)A13 - 27
3X-RAY DIFFRACTION3(chain A and resid 28:109)A28 - 109
4X-RAY DIFFRACTION4(chain A and resid 110:140)A110 - 140
5X-RAY DIFFRACTION5(chain A and resid 141:150)A141 - 150
6X-RAY DIFFRACTION6(chain A and resid 151:9999)A - B151 - 9999
7X-RAY DIFFRACTION7(chain B and resid 0:15)B0 - 15
8X-RAY DIFFRACTION8(chain B and resid 16:31)B16 - 31
9X-RAY DIFFRACTION9(chain B and resid 32:97)B32 - 97
10X-RAY DIFFRACTION10(chain B and resid 98:116)B98 - 116
11X-RAY DIFFRACTION11(chain B and resid 117:138)B117 - 138
12X-RAY DIFFRACTION12(chain B and resid 139:223)B139 - 223

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more