› 2f8v

X-ray diffraction
2.75Å resolution

Structure of full length telethonin in complex with the N-terminus of titin

Released:
DOI: 10.2210/pdb2f8v/pdb
PDB entry 2f8v coloured by chain, front view.
PDB entry 2f8v coloured by chain, side view.
PDB entry 2f8v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus.
Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M
J Struct Biol 155 239-50 (2006)
PMID: 16713295

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127406 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Titin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 201 amino acids
Theoretical weight: 21.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WZ42 (Residues: 1-196; Coverage: 1%)
Gene name: TTN
Sequence domains: Immunoglobulin I-set domain
Structure domains: Immunoglobulins
Telethonin Chains: T, Y
Molecule details ›
Chains: T, Y
Length: 167 amino acids
Theoretical weight: 18.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15273 (Residues: 1-167; Coverage: 100%)
Gene name: TCAP
Sequence domains: Telethonin protein
Structure domains: titin domain like

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 112.513Å b: 46.885Å c: 128.033Å
α: 90° β: 98.3° γ: 90°
R-values:
R R work R free
0.266 0.267 0.287
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Muscle giants: molecular scaffolds in sarcomerogenesis.
Kontrogianni-Konstantopoulos et al. (2009)
3 more

1 mention without citation

Mechanosignaling pathways alter muscle structure and function by post-translational modification of existing sarcomeric proteins to optimize energy usage.
Russell et al. (2021)