Structure of IDP90555

Crystal Structure of Tryptophanyl-tRNA Synthetase from Campylobacter jejuni complexed with ADP and Tryptophane

Edit deposit information
CSGID target
IDP90555 
PDB Id
3TZL (NCBI MMDB
Authors
Y.Kim,M.Zhou,S.Grimshaw,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Youngchang Kim 
Responsible lab
Argonne National Laboratory 
Deposition Date
Sep 27, 2011 
Release Date
Oct 05, 2011 

Annotation

Description
Tryptophanyl-tRNA Synthetase (TrpS) is involved in protein synthesis and regulation of RNA transcription and translation. It catalyzes a two-step reaction, first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA. The structure was produced by co-crystallizing the protein with ADP, however, not only ADP but also Trp were found bound tightly in the active site located in the middle of each subunit of the dimer. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
PO4 PHOSPHATE ION crystallization
LTR l-tryptophan biological
ADP biological
MSE modified residue
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=66.78Å, b=50.63Å, c=105.92Å
α=90.00, β=107.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
28.79-2.15Å (2.21-2.15Å)  
Rall(%)
18.3 
Rwork(%)
18.1 (24.0) 
Rfree(%)
21.8 (28.3) 
Num. observed reflections
38111 (2299) 
Num. Rfree reflections
1901 (113) 
Completeness(%)
98.1 (82.0) 

Model parameters

Num Atoms
5135  
Num Waters
218  
Num Hetatoms
294  
Model mean isotropic B factor
49.070Å2  
RMSD bond length
0.009Å  
RMSD bond angle
1.189°  
RMSD dihedral angle
15.417°
 
Filename uploaded
dep.pdb (uploaded on Sep 27, 2011 2:18 PM)  
Inserted
Sep 27, 2011