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- PDB-30uc: Complex of transglutaminase 2 and the 45 kDa domain of fibronectin -

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Basic information

Entry
Database: PDB / ID: 30uc
TitleComplex of transglutaminase 2 and the 45 kDa domain of fibronectin
Components
  • Fibronectin
  • Protein-glutamine gamma-glutamyltransferase 2
KeywordsTRANSFERASE / transglutaminase / fibronectin
Function / homology
Function and homology information


peptide serotonyltransferase activity / histone serotonyltransferase activity / peptide dopaminyltransferase activity / histone dopaminyltransferase activity / peptide noradrenalinyltransferase activity / peptide histaminyltransferase activity / regulation of apoptotic cell clearance / negative regulation of endoplasmic reticulum calcium ion concentration / cellular response to serotonin / protein-glutamine glutaminase activity ...peptide serotonyltransferase activity / histone serotonyltransferase activity / peptide dopaminyltransferase activity / histone dopaminyltransferase activity / peptide noradrenalinyltransferase activity / peptide histaminyltransferase activity / regulation of apoptotic cell clearance / negative regulation of endoplasmic reticulum calcium ion concentration / cellular response to serotonin / protein-glutamine glutaminase activity / protein-glutamine glutaminase / protein-glutamine gamma-glutamyltransferase / fibronectin fibril / negative regulation of monocyte activation / protein-glutamine gamma-glutamyltransferase activity / peptide cross-linking / negative regulation of transforming growth factor beta production / positive regulation of substrate-dependent cell migration, cell attachment to substrate / cell-substrate junction assembly / neural crest cell migration involved in autonomic nervous system development / fibrinogen complex / blood coagulation, fibrin clot formation / Fibronectin matrix formation / enteric nervous system development / Attachment of bacteria to epithelial cells / positive regulation of small GTPase mediated signal transduction / integrin activation / cellular response to dopamine / neural crest cell migration / ALK mutants bind TKIs / non-collagenous component of basement membrane / positive regulation of mitochondrial calcium ion concentration / cellular response to cocaine / proteoglycan binding / apoptotic cell clearance / positive regulation of neurogenesis / Molecules associated with elastic fibres / MET activates PTK2 signaling / endodermal cell differentiation / Hydrolases; Acting on peptide bonds (peptidases) / response to muscle activity / Syndecan interactions / p130Cas linkage to MAPK signaling for integrins / peptidase activator activity / extracellular matrix structural constituent / biological process involved in interaction with symbiont / positive regulation of sprouting angiogenesis / endoplasmic reticulum-Golgi intermediate compartment / GRB2:SOS provides linkage to MAPK signaling for Integrins / regulation of protein phosphorylation / Non-integrin membrane-ECM interactions / Integrin cell surface interactions / regulation of ERK1 and ERK2 cascade / ECM proteoglycans / endothelial cell migration / substrate adhesion-dependent cell spreading / extracellular matrix organization / cell-matrix adhesion / Degradation of the extracellular matrix / collagen binding / Integrin signaling / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / GTPase activator activity / positive regulation of cell adhesion / integrin-mediated signaling pathway / platelet alpha granule lumen / positive regulation of fibroblast proliferation / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / Cell surface interactions at the vascular wall / Developmental Lineage of Pancreatic Ductal Cells / Post-translational protein phosphorylation / bone development / response to wounding / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / protein homooligomerization / integrin binding / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / heart development / heparin binding / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / phospholipase C-activating G protein-coupled receptor signaling pathway / nervous system development / Signaling by BRAF and RAF1 fusions / Signaling by ALK fusions and activated point mutants / Platelet degranulation / GPER1 signaling / protease binding / cell adhesion / Interleukin-4 and Interleukin-13 signaling / blood microparticle / extracellular matrix / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / regulation of apoptotic process / apical plasma membrane / positive regulation of apoptotic process / receptor ligand activity
Similarity search - Function
Transglutaminase, N-terminal / Transglutaminase, C-terminal / Transglutaminase, active site / Protein-glutamine gamma-glutamyltransferase, animal / Transglutaminase, C-terminal domain superfamily / : / Transglutaminase family / Transglutaminase family, C-terminal ig like domain / Transglutaminases active site. / Transglutaminase-like superfamily ...Transglutaminase, N-terminal / Transglutaminase, C-terminal / Transglutaminase, active site / Protein-glutamine gamma-glutamyltransferase, animal / Transglutaminase, C-terminal domain superfamily / : / Transglutaminase family / Transglutaminase family, C-terminal ig like domain / Transglutaminases active site. / Transglutaminase-like superfamily / Transglutaminase/protease-like homologues / Transglutaminase-like / Fibronectin type I domain / Fibronectin, type I / Fibronectin type-I domain signature. / Fibronectin type-I domain profile. / Fibronectin type 1 domain / : / Transglutaminase-like superfamily / Fibronectin type II domain / Fibronectin type II domain superfamily / Fibronectin type II domain / Fibronectin type-II collagen-binding domain signature. / Fibronectin type-II collagen-binding domain profile. / Fibronectin type 2 domain / Kringle-like fold / Fibronectin type III domain / EGF-like domain signature 1. / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Papain-like cysteine peptidase superfamily / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin E-set / Immunoglobulin-like fold
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Fibronectin / Protein-glutamine gamma-glutamyltransferase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsHeggelund, J.E. / Ali-Ahmad, A. / Sekulic, N. / Sollid, L.M.
Funding support Denmark, Norway, 2items
OrganizationGrant numberCountry
Other privateLF-OC-23-001291 Denmark
Research Council of Norway295844 Norway
CitationJournal: J Biol Chem / Year: 2026
Title: Cryo-EM structure of the complex between transglutaminase 2 and the 45 kDa domain of fibronectin.
Authors: Julie Elisabeth Heggelund / Ahmad Ali-Ahmad / Marie Kongshaug Johannesen / Nikolina Sekulić / Ludvig M Sollid /
Abstract: Fibronectin (FN) and transglutaminase 2 (TG2) engage in a high-affinity interaction. This interaction affects anchoring, migration and survival of cells, and high cellular expression of TG2 is ...Fibronectin (FN) and transglutaminase 2 (TG2) engage in a high-affinity interaction. This interaction affects anchoring, migration and survival of cells, and high cellular expression of TG2 is associated with metastasis potential of cancers. Previous work has mapped the interaction to involve the N-terminal part of TG2 and an N-terminally located 45 kDa domain of FN (FN45). In particular, the I module of FN45 is reported to be necessary and sufficient for TG2 binding. Here, we present the cryo-EM structure of a complex between human TG2 and FN45 at 2.8 Å resolution. In the structure, the distal region of the TG2 N-terminal domain binds the FN45 I module, whereas the proximal N-terminal region and adjacent catalytic core segment bind the FN45 I module and, to a lesser extent, the FN45 II module. The FN45 I and FN45 I modules have about equal buried surface areas in their interaction with TG2. A glycine residue at position 127 of TG2 is crucial for interaction with Trp553 of the FN45 I module. Mutation of this residue to isoleucine, which is carried by transglutaminase 3 that does not bind FN45, abrogates the binding of FN45 to TG2. This finding suggests that the interaction of the FN45 I module with TG2 is contingent on the FN45 I module making an interaction with TG2. Further, this finding highlights the region surrounding residue 127 of TG2 as a promising target for structure-based design of anticancer drugs aimed at disrupting the TG2-FN interaction.
History
DepositionMay 13, 2026Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 22, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein-glutamine gamma-glutamyltransferase 2
B: Fibronectin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)115,6965
Polymers114,8102
Non-polymers8863
Water97354
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Protein-glutamine gamma-glutamyltransferase 2 / Erythrocyte transglutaminase / Heart G alpha(h) / hhG alpha(h) / Isopeptidase TGM2 / Protein G ...Erythrocyte transglutaminase / Heart G alpha(h) / hhG alpha(h) / Isopeptidase TGM2 / Protein G alpha(h) / G(h) / Protein-glutamine deamidase TGM2 / Protein-glutamine dopaminyltransferase TGM2 / Protein-glutamine histaminyltransferase TGM2 / Protein-glutamine noradrenalinyltransferase TGM2 / Protein-glutamine serotonyltransferase TGM2 / Tissue transglutaminase / tTG / tTgase / Transglutaminase C / TG(C) / TGC / TGase C / Transglutaminase H / TGase H / Transglutaminase II / TGase II / Transglutaminase-2 / TG2 / TGase-2 / hTG2


Mass: 80416.953 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TGM2 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P21980, protein-glutamine gamma-glutamyltransferase, Hydrolases; Acting on peptide bonds (peptidases), protein-glutamine glutaminase, Transferases; Acyltransferases; Transferring ...References: UniProt: P21980, protein-glutamine gamma-glutamyltransferase, Hydrolases; Acting on peptide bonds (peptidases), protein-glutamine glutaminase, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups
#2: Protein Fibronectin / FN / Cold-insoluble globulin / CIG


Mass: 34392.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P02751
#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 54 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Complex of transglutaminase 2 and the 45 kDa fragment of fibronectin
Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightValue: 125 kDa/nm / Experimental value: YES
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1
VitrificationCryogen name: ETHANE / Humidity: 100 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 600 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
12cryoSPARC3D reconstruction
13PHENIX2.0_5936model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 238000 / Symmetry type: POINT
Atomic model buildingB value: 74 / Protocol: OTHER
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 74.23 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00146615
ELECTRON MICROSCOPYf_angle_d0.38678975
ELECTRON MICROSCOPYf_chiral_restr0.0397974
ELECTRON MICROSCOPYf_plane_restr0.00231168
ELECTRON MICROSCOPYf_dihedral_angle_d3.6289935

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