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Structure of IDP00047

1.6 Angstrom resolution crystal structure of putative streptothricin acetyltransferase from Bacillus anthracis str. Ames in complex with acetyl coenzyme A

Edit deposit information
CSGID target
IDP00047 
PDB Id
3PP9 (NCBI MMDB
Authors
A.S.Halavaty,Z.Wawrzak,O.Onopriyenko,A.Edwards,A.Savchenko,S.Peterson,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Andrei Halavaty 
Responsible lab
Northwestern University 
Deposition Date
Nov 24, 2010 
Release Date
Jan 12, 2011 

Annotation

Description
The structure of the putative Se-Met streptothricin acetyltransferase from Bacillus anthracis str. Ames in complex with acetyl coenzyme A was solved by SAD. The protein is mostly β-stranded (40 %) with 20 % of the helical component. The core of the enzyme is a six-stranded antiparallel β-sheet, which ideal alignment is disrupted by the aliphatic tail of Acetyl-CoA. The tail mimics β-strand-β-strand hydrogen bonding interactions, making the sheet quasi seven-stranded. Each of three copies of the protein binds a single Acetyl-CoA molecule, which electron density is well defined. The chains B and C form a dimer with the buried surface area of 2140 A2, whereas chain A makes identical dimer with a symmetry related molecule with 2480 A2 of buried surface area. Monomers in the dimer interact such a way that a six-stranded antiparallel β-sheet is formed.  
Functional assignment
Transferase 

Ligands

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

Structure information

Unit cell parameters

Space Group
C 1 2 1  
Unit Cell

a=47.10Å, b=68.01Å, c=174.17Å
α=90.00, β=97.61, γ=90.00 
Solvent content
41.18  
Matthews coefficient
2.09  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.28-1.60Å (1.64-1.60Å)  
Rall(%)
19.0 
Rwork(%)
18.9 (22.9) 
Rfree(%)
22.2 (25.1) 
Num. observed reflections
70882 (4357) 
Num. Rfree reflections
3544 (218) 
Completeness(%)
98.4 (82.9) 

Model parameters

Num Atoms
4568  
Num Waters
355  
Num Hetatoms
686  
Model mean isotropic B factor
28.640Å2  
RMSD bond length
0.010Å  
RMSD bond angle
1.591°  
Filename uploaded
3PP9.pdb (uploaded on Sep 28, 2011 11:11 AM)  
Inserted
Dec 06, 2010