Annotation

Description

Cyclic adenosine monophosphate (cAMP, cyclic AMP or 3'-5'-cyclic adenosine monophosphate) is an important signaling molecule in virtually all prokaryotic and eukaryotic cells. It activates diverse bacterial cAMP receptor proteins such as transcription factors and protein kinases. cAMP is derived from adenosine triphosphate (ATP) in reaction catalyzed by adenylate cyclase (AC). There are six distinct non-homologous classes of ACs. The majority of enzymes belong to class III which converts ATP to cAMP in a catalytic center formed by an interface of protein homodimers. GBAA_1210 protein monomer structure has the same fold as class IV AC from Yersinia pestis (3N10 deposit in PDB); however, it displays a different dimer organization at least inside crystals. The Y. pestis AC monomer forms an antiparallel eight-stranded barrel which binds ligands inside the barrel. The presented structure is complexed with AMP which is neither a substrate nor product for adenylate cyclase. That is why the complex could be an artifact of crystallization. An AMP molecule is bound on a monomer surface close to an interface with other molecule from a protein dimer. 

Functional assignment

 

Structure information

Unit cell parameters

Space Group

P 1 21 1  

Unit Cell

a=67.23Å, b=86.31Å, c=76.44Å
α=90.00, β=102.02, γ=90.00 

Solvent content

 

Matthews coefficient

 

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

38.00-2.10Å (2.16-2.10Å)  

R_all(%)

19.5 

R_work(%)

19.3 (28.1) 

R_free(%)

24.5 (32.7) 

Num. observed reflections

48535 (2839) 

Num. R_free reflections

2426 (149) 

Completeness(%)

97.7 (78.3) 

Model parameters

Num Atoms

6154  

Num Waters

234  

Num Hetatoms

0  

Model mean isotropic B factor

34.330Ų  

RMSD bond length

0.019Å  

RMSD bond angle

1.717°  

Filename uploaded

idp02500_amp.pdb (uploaded on Aug 23, 2011 7:41 PM)  

Inserted

Aug 23, 2011