› 4tvb

X-ray diffraction
1.69Å resolution

Crystal Structure of the Homospermidine Synthase (HSS) from Blastochloris viridis in Complex with NAD, Putrescine and sym-Homospermidine

Released:
DOI: 10.2210/pdb4tvb/pdb
PDB entry 4tvb coloured by chain, front view.
PDB entry 4tvb coloured by chain, side view.
PDB entry 4tvb coloured by chain, top view.
Source organism: Blastochloris viridis
Primary publication:
Comprehensive Structural Characterization of the Bacterial Homospermidine Synthase-an Essential Enzyme of the Polyamine Metabolism.
Krossa S, Faust A, Ober D, Scheidig AJ
Sci Rep 6 19501 (2016)
PMID: 26776105

Function and Biology Details

Reaction catalysed: 
2 putrescine = sym-homospermidine + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homospermidine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 479 amino acids
Theoretical weight: 52.98 KDa
Source organism: Blastochloris viridis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O32323 (Residues: 1-477; Coverage: 100%)
Gene name: hss
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 1 x NAI

Cofactor: Ligand NAD 1 x NAD
3 bound ligands:
Ligand 37Z 1 x 37Z
Ligand 1PS 1 x 1PS
Ligand PUT 1 x PUT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Unit cell:
a: 59.51Å b: 109.254Å c: 157.212Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Antibacterial Diamines Targeting Bacterial Membranes.
Wang et al. (2016)
4 more

2 mentions without citation

Comprehensive Structural Characterization of the Bacterial Homospermidine Synthase-an Essential Enzyme of the Polyamine Metabolism.
Krossa et al. (2016)
1 more