› 5jju

X-ray diffraction
2.31Å resolution

Crystal structure of Rv2837c complexed with 5'-pApA and 5'-AMP

Released:
DOI: 10.2210/pdb5jju/pdb
PDB entry 5jju coloured by chain, front view.
PDB entry 5jju coloured by chain, side view.
PDB entry 5jju coloured by chain, top view.
Source organisms:
Primary publication:
Structural and biochemical insight into the mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP phosphodiesterase.
He Q, Wang F, Liu S, Zhu D, Cong H, Gao F, Li B, Wang H, Lin Z, Liao J, Gu L
J Biol Chem 291 14386-14387 (2016)
PMID: 27371563

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107747 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Uncharacterized protein Rv2837c Chains: A, B
Molecule details ›
Chains: A, B
Length: 340 amino acids
Theoretical weight: 35.76 KDa
Source organism: Mycobacterium tuberculosis H37Ra
Expression system: Escherichia coli
UniProt:
  • Canonical: A5U6I9 (Residues: 11-336; Coverage: 97%)
Gene name: MRA_2860
Sequence domains:
RNA (5'-R(P*AP*A)-3') Chain: C
Molecule details ›
Chain: C
Length: 2 nucleotides
Theoretical weight: 613 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MN 4 x MN
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 58.374Å b: 99.267Å c: 108.677Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.217 0.288
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

c-di-AMP: An Essential Molecule in the Signaling Pathways that Regulate the Viability and Virulence of Gram-Positive Bacteria.
Fahmi et al. (2017)
8 other articles

5 mentions without citation

Making and Breaking of an Essential Poison: the Cyclases and Phosphodiesterases That Produce and Degrade the Essential Second Messenger Cyclic di-AMP in Bacteria.
Commichau et al. (2019)
4 more