› 6z1n

X-ray diffraction
2.3Å resolution

Structure of the human heterotetrameric cis-prenyltransferase complex

Released:
DOI: 10.2210/pdb6z1n/pdb
PDB entry 6z1n coloured by chain, front view.
PDB entry 6z1n coloured by chain, side view.
PDB entry 6z1n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.
Bar-El ML, Vaňková P, Yeheskel A, Simhaev L, Engel H, Man P, Haitin Y, Giladi M
OpenAccess logo Nat Commun 11 5273 (2020)
PMID: 33077723

Function and Biology Details

Reaction catalysed: 
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183153 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dehydrodolichyl diphosphate synthase complex subunit DHDDS Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 39.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86SQ9 (Residues: 1-333; Coverage: 100%)
  • Best match: Q86SQ9-2 (Residues: 1-334)
Gene names: DHDDS, HDS
Sequence domains: Putative undecaprenyl diphosphate synthase
Dehydrodolichyl diphosphate synthase complex subunit NUS1 Chain: B
Molecule details ›
Chain: B
Length: 219 amino acids
Theoretical weight: 24.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96E22 (Residues: 73-293; Coverage: 72%)
Gene names: C6orf68, NGBR, NUS1
Sequence domains: Putative undecaprenyl diphosphate synthase

Ligands and Environments

3 bound ligands:
Ligand FPP 1 x FPP
Ligand PO4 1 x PO4
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: R32
Unit cell:
a: 184.074Å b: 184.074Å c: 112.593Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.189 0.223
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Perspectives on Retinal Dolichol Metabolism, and Visual Deficits in Dolichol Metabolism-Associated Inherited Disorders.
Rao et al. (2023)
1 more

1 mention without citation

Structural basis for long-chain isoprenoid synthesis by cis-prenyltransferases.
Giladi et al. (2022)