› 4o4s

X-ray diffraction
2.5Å resolution

Crystal structure of phycobiliprotein lyase CpcT complexed with phycocyanobilin (PCB)

Released:
DOI: 10.2210/pdb4o4s/pdb
PDB entry 4o4s coloured by chain, front view.
PDB entry 4o4s coloured by chain, side view.
PDB entry 4o4s coloured by chain, top view.
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Primary publication:
Structure and mechanism of the phycobiliprotein lyase CpcT.
Zhou W, Ding WL, Zeng XL, Dong LL, Zhao B, Zhou M, Scheer H, Zhao KH, Yang X
J Biol Chem 289 26677-26689 (2014)
PMID: 25074932

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187074 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phycocyanobilin lyase CpcT Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 207 amino acids
Theoretical weight: 24.25 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8YLF9 (Residues: 1-199; Coverage: 100%)
Gene names: all5339, cpcT1, cpeT1
Sequence domains: CpeT/CpcT family (DUF1001)
Structure domains: CpcT/CpeT domain

Ligands and Environments

1 bound ligand:
Ligand CYC 12 x CYC
1 modified residue:
Ligand MSE 72 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P1
Unit cell:
a: 69.746Å b: 69.601Å c: 162.595Å
α: 90.21° β: 90.28° γ: 60.12°
R-values:
R R work R free
0.184 0.18 0.248
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions.
Li et al. (2023)
9 other articles

5 mentions without citation

Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.
Zhao et al. (2017)
4 more