› 1jog

X-ray diffraction
2.4Å resolution

Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase

Released:
DOI: 10.2210/pdb1jog/pdb
PDB entry 1jog coloured by chain, front view.
PDB entry 1jog coloured by chain, side view.
PDB entry 1jog coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
The HI0073/HI0074 protein pair from Haemophilus influenzae is a member of a new nucleotidyltransferase family: structure, sequence analyses, and solution studies.
Lehmann C, Lim K, Chalamasetty VR, Krajewski W, Melamud E, Galkin A, Howard A, Kelman Z, Reddy PT, Murzin AG, Herzberg O
Proteins 50 249-60 (2003)
PMID: 12486719

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155161 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable ribonuclease HepT Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 146 amino acids
Theoretical weight: 17.52 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43934 (Residues: 1-146; Coverage: 100%)
Gene names: HI_0074, hepT
Sequence domains: Nucleotidyltransferase substrate binding protein like
Structure domains: Nucleotidyltransferases domain 2

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 38.3Å b: 87.1Å c: 165.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.282
Expression system: Escherichia coli

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Citations

2 review citations

Comparative genomics of Archaea: how much have we learned in six years, and what's next?
Makarova et al. (2003)
1 more

9 mentions without citation

RNA-specific ribonucleotidyl transferases.
Martin et al. (2007)
8 more