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- PDB-5tx2: Miniature TGF-beta2 3-mutant monomer -

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Basic information

Entry
Database: PDB / ID: 5tx2
TitleMiniature TGF-beta2 3-mutant monomer
ComponentsTransforming growth factor beta-2
KeywordsCYTOKINE / Growth factor
Function / homology
Function and homology information


positive regulation of activation-induced cell death of T cells / positive regulation of GTP binding / TGFBR3 regulates TGF-beta signaling / Molecules associated with elastic fibres / regulation of timing of catagen / regulation of apoptotic process involved in outflow tract morphogenesis / substantia propria of cornea development / negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / ascending aorta morphogenesis / negative regulation of keratinocyte differentiation ...positive regulation of activation-induced cell death of T cells / positive regulation of GTP binding / TGFBR3 regulates TGF-beta signaling / Molecules associated with elastic fibres / regulation of timing of catagen / regulation of apoptotic process involved in outflow tract morphogenesis / substantia propria of cornea development / negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / ascending aorta morphogenesis / negative regulation of keratinocyte differentiation / embryonic neurocranium morphogenesis / cardioblast differentiation / positive regulation of timing of catagen / TGF-beta receptor signaling activates SMADs / positive regulation of cardioblast differentiation / negative regulation of cartilage development / somatic stem cell division / regulation of extracellular matrix organization / atrial septum morphogenesis / heart valve morphogenesis / cardiac right ventricle morphogenesis / pericyte cell differentiation / regulation of transforming growth factor beta2 production / transforming growth factor beta complex / uterus development / positive regulation of heart contraction / pharyngeal arch artery morphogenesis / negative regulation of macrophage cytokine production / glial cell migration / type III transforming growth factor beta receptor binding / positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / positive regulation of stress-activated MAPK cascade / cardiac left ventricle morphogenesis / salivary gland morphogenesis / atrial septum primum morphogenesis / positive regulation of extracellular matrix disassembly / membranous septum morphogenesis / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / secondary palate development / positive regulation of integrin biosynthetic process / endocardial cushion fusion / hair follicle development / positive regulation of cardiac epithelial to mesenchymal transition / cranial skeletal system development / cardiac epithelial to mesenchymal transition / embryonic limb morphogenesis / neuron fate commitment / signaling / Platelet degranulation / eye development / embryonic digestive tract development / cell-cell junction organization / type II transforming growth factor beta receptor binding / pulmonary valve morphogenesis / transforming growth factor beta receptor binding / negative regulation of Ras protein signal transduction / neural retina development / atrioventricular valve morphogenesis / ventricular trabecula myocardium morphogenesis / collagen fibril organization / outflow tract septum morphogenesis / hair follicle morphogenesis / blood vessel development / endocardial cushion morphogenesis / face morphogenesis / positive regulation of cell adhesion mediated by integrin / negative regulation of release of sequestered calcium ion into cytosol / cartilage condensation / ventricular septum morphogenesis / neural tube closure / blood vessel remodeling / positive regulation of Notch signaling pathway / dopamine biosynthetic process / inner ear development / hemopoiesis / outflow tract morphogenesis / response to progesterone / positive regulation of epithelial cell migration / positive regulation of cell division / cardiac muscle cell proliferation / positive regulation of SMAD protein signal transduction / basement membrane / neuron development / heart morphogenesis / epithelial to mesenchymal transition / skeletal system development / transforming growth factor beta receptor signaling pathway / positive regulation of epithelial to mesenchymal transition / extrinsic apoptotic signaling pathway / extracellular matrix organization / cell morphogenesis / neutrophil chemotaxis / kidney development / negative regulation of angiogenesis / epithelial cell differentiation / male gonad development / positive regulation of cell cycle / secretory granule / axon guidance / cytokine activity
Similarity search - Function
Transforming growth factor beta-2 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain ...Transforming growth factor beta-2 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Cystine-knot cytokine
Similarity search - Domain/homology
Transforming growth factor beta-2 proprotein
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.82 Å
AuthorsTaylor, A.B. / Kim, S.K. / Hart, P.J. / Hinck, A.P.
CitationJournal: J. Biol. Chem. / Year: 2017
Title: An engineered transforming growth factor beta (TGF-beta ) monomer that functions as a dominant negative to block TGF-beta signaling.
Authors: Kim, S.K. / Barron, L. / Hinck, C.S. / Petrunak, E.M. / Cano, K.E. / Thangirala, A. / Iskra, B. / Brothers, M. / Vonberg, M. / Leal, B. / Richter, B. / Kodali, R. / Taylor, A.B. / Du, S. / ...Authors: Kim, S.K. / Barron, L. / Hinck, C.S. / Petrunak, E.M. / Cano, K.E. / Thangirala, A. / Iskra, B. / Brothers, M. / Vonberg, M. / Leal, B. / Richter, B. / Kodali, R. / Taylor, A.B. / Du, S. / Barnes, C.O. / Sulea, T. / Calero, G. / Hart, P.J. / Hart, M.J. / Demeler, B. / Hinck, A.P.
History
DepositionNov 15, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 1, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 8, 2017Group: Database references
Revision 1.2May 10, 2017Group: Database references
Revision 1.3Oct 4, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transforming growth factor beta-2
B: Transforming growth factor beta-2


Theoretical massNumber of molelcules
Total (without water)21,2072
Polymers21,2072
Non-polymers00
Water1,928107
1
A: Transforming growth factor beta-2


Theoretical massNumber of molelcules
Total (without water)10,6031
Polymers10,6031
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Transforming growth factor beta-2


Theoretical massNumber of molelcules
Total (without water)10,6031
Polymers10,6031
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)99.459, 33.355, 54.131
Angle α, β, γ (deg.)90.00, 109.55, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-253-

HOH

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Components

#1: Protein Transforming growth factor beta-2 / TGF-beta-2


Mass: 10603.290 Da / Num. of mol.: 2 / Fragment: UNP residues 303-414 / Mutation: L51R,A74K,C77S
Source method: isolated from a genetically manipulated source
Details: Residues 52-71 were deleted. / Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tgfb2 / Production host: Escherichia coli (E. coli) / References: UniProt: P27090
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 107 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.02 Å3/Da / Density % sol: 39.11 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / Details: 20% PEG 3350, 0.2 M sodium thiocyanate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 6, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.82→51.01 Å / Num. obs: 15033 / % possible obs: 98.4 % / Redundancy: 3.6 % / Biso Wilson estimate: 28.9 Å2 / Rsym value: 0.05 / Net I/σ(I): 12.7
Reflection shellResolution: 1.82→1.92 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.443 / Mean I/σ(I) obs: 2.2 / % possible all: 98.4

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Processing

Software
NameVersionClassification
PHENIX1.10_2155refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2TGI

2tgi


Resolution: 1.82→51.01 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.4 / Phase error: 27.94
RfactorNum. reflection% reflection
Rfree0.2519 1503 10 %
Rwork0.2091 --
obs0.2133 15027 98.15 %
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å
Refinement stepCycle: LAST / Resolution: 1.82→51.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1462 0 0 107 1569
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0121508
X-RAY DIFFRACTIONf_angle_d1.032050
X-RAY DIFFRACTIONf_dihedral_angle_d12.902582
X-RAY DIFFRACTIONf_chiral_restr0.064214
X-RAY DIFFRACTIONf_plane_restr0.007262
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.82-1.87870.35691350.30221216X-RAY DIFFRACTION98
1.8787-1.94590.29411360.25651229X-RAY DIFFRACTION99
1.9459-2.02380.32051340.23181211X-RAY DIFFRACTION99
2.0238-2.11590.32951370.21471228X-RAY DIFFRACTION99
2.1159-2.22750.27631370.22191232X-RAY DIFFRACTION99
2.2275-2.3670.32521370.22421227X-RAY DIFFRACTION98
2.367-2.54980.28651350.21531218X-RAY DIFFRACTION99
2.5498-2.80640.28451370.23221237X-RAY DIFFRACTION99
2.8064-3.21240.25071380.21241237X-RAY DIFFRACTION98
3.2124-4.0470.21011350.19371219X-RAY DIFFRACTION96
4.047-51.03040.21021420.18631270X-RAY DIFFRACTION97

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