› 1yk9

X-ray diffraction
2.7Å resolution

Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c

Released:
DOI: 10.2210/pdb1yk9/pdb
PDB entry 1yk9 coloured by chain, front view.
PDB entry 1yk9 coloured by chain, side view.
PDB entry 1yk9 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis.
Ketkar AD, Shenoy AR, Ramagopal UA, Visweswariah SS, Suguna K
J Mol Biol 356 904-16 (2006)
PMID: 16403515

Function and Biology Details

Reaction catalysed: 
ATP = 3',5'-cyclic AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162041 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate cyclase Chain: A
Molecule details ›
Chain: A
Length: 204 amino acids
Theoretical weight: 22.37 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P9WQ35 (Residues: 240-443; Coverage: 46%)
Gene names: MTCY01B2.17c, Rv1625c, cya
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P41
Unit cell:
a: 71.02Å b: 71.02Å c: 43.739Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.245
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Molecular details of cAMP generation in mammalian cells: a tale of two systems.
Kamenetsky et al. (2006)
3 more

1 mention without citation

New structural forms of a mycobacterial adenylyl cyclase Rv1625c.
Barathy et al. (2014)