› 1ykd

X-ray diffraction
1.9Å resolution

Crystal Structure of the Tandem GAF Domains from a Cyanobacterial Adenylyl Cyclase: Novel Modes of Ligand-Binding and Dimerization

Released:
DOI: 10.2210/pdb1ykd/pdb
PDB entry 1ykd coloured by chain, front view.
PDB entry 1ykd coloured by chain, side view.
PDB entry 1ykd coloured by chain, top view.
Source organism: Anabaena sp.
Primary publication:
Crystal structure of the tandem GAF domains from a cyanobacterial adenylyl cyclase: modes of ligand binding and dimerization.
Martinez SE, Bruder S, Schultz A, Zheng N, Schultz JE, Beavo JA, Linder JU
Proc Natl Acad Sci U S A 102 3082-7 (2005)
PMID: 15708973

Function and Biology Details

Reaction catalysed: 
ATP = 3',5'-cyclic AMP + diphosphate
Biochemical function:
  • not assigned
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-161095 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate cyclase Chains: A, B
Molecule details ›
Chains: A, B
Length: 398 amino acids
Theoretical weight: 44.93 KDa
Source organism: Anabaena sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P94182 (Residues: 58-445; Coverage: 45%)
Gene name: cyaB2
Sequence domains: GAF domain
Structure domains: Beta-Lactamase

Ligands and Environments

1 bound ligand:
Ligand CMP 4 x CMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 61.958Å b: 66.265Å c: 70.212Å
α: 103.57° β: 96.56° γ: 115.15°
R-values:
R R work R free
0.184 0.182 0.215
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Biochemistry and physiology of cyclic nucleotide phosphodiesterases: essential components in cyclic nucleotide signaling.
Conti et al. (2007)
12 more

10 mentions without citation

Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.
Gushchin et al. (2021)
9 more