To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP00836

1.25 ANGSTROM CRYSTAL STRUCTURE OF PYRROLIDONE-CARBOXYLATE PEPTIDASE (PCP) FROM STAPHYLOCOCCUS AUREUS

Edit deposit information
CSGID target
IDP00836 
PDB Id
3GIU (NCBI MMDB
Authors
G.Minasov,Z.Wawrzak,T.Skarina,O.Onopriyenko,S.N.Peterson,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Mar 06, 2009 
Release Date
Mar 17, 2009 

Annotation

Description
Pyroglutamyl peptidase (PGP) type I, also known as Pyrrolidone-Carboxylate Peptidase (PCP), is an enzyme that selectively removes pyrrolidone carboxylic acid (PCA), also called pyroglutamate (pGlu), from N-terminus of peptides and proteins. N-terminal glutamine residue can spontaneously become pyroglutamate (pGlu), and protect these proteins from proteolysis by other proteases until a PCP removes the pGlu. The PCP is common in many bacteria, and less usual for plant, animal and human tissues. The enzyme belongs to the cysteine peptidase family, with the common Cys-His-Asp catalytic triad. There are several structures of homologous proteins deposited in the PDB, which are homo tetramers and it was postulated that the functional unit is a tetramer. In this crystal structure of PCP from Staphylococcus aureus, the protein forms dimer. It is not clear whether the functional form is a monomer, dimer, or tetramer. The product of hydrolysis, a Pyroglutamic Acid, improves blood circulation in the brain, and is sold as “smart drug”. Derivatives of PCA, Pyrrolidones, are used for neuroprotection after stroke and as antiepileptic agents.  
Functional assignment
Pyrrolidone-Carboxylate Peptidase 

Ligands

Ligand code Name Ligand type
GOL
PEG
ZN
PG4
MSE modified residue
ACY

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=42.79Å, b=81.00Å, c=119.91Å
α=90.00, β=90.00, γ=90.00 
Solvent content
44.12  
Matthews coefficient
2.2  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
24.55-1.25Å (1.28-1.25Å)  
Rall(%)
11.8 
Rwork(%)
11.6 (21.7) 
Rfree(%)
14.8 (23.8) 
Num. observed reflections
113996 (7426) 
Num. Rfree reflections
5699 (369) 
Completeness(%)
98.3 (87.9) 

Model parameters

Num Atoms
3500  
Num Waters
619  
Num Hetatoms
862  
Model mean isotropic B factor
9.120Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.459°  
Filename uploaded
rcsb051914.pdb (uploaded on Mar 26, 2009 10:49 AM)  
Inserted
Mar 26, 2009