3A54: Crystal Structure Of The A47q1 Mutant Of Pro-Protein-Glutaminase

Citation:
Abstract
Protein glutaminase, which converts a protein glutamine residue to a glutamate residue, is expected to be useful as a new food-processing enzyme. The crystal structures of the mature and pro forms of the enzyme were refined at 1.15 and 1.73 A resolution, respectively. The overall structure of the mature enzyme has a weak homology to the core domain of human transglutaminase-2. The catalytic triad (Cys-His-Asp) common to transglutaminases and cysteine proteases is located in the bottom of the active site pocket. The structure of the recombinant pro form shows that a short loop between S2 and S3 in the proregion covers and interacts with the active site of the mature region, mimicking the protein substrate of the enzyme. Ala-47 is located just above the pocket of the active site. Two mutant structures (A47Q-1 and A47Q-2) refined at 1.5 A resolution were found to correspond to the enzyme-substrate complex and an S-acyl intermediate. Based on these structures, the catalytic mechanism of protein glutaminase is proposed.
PDB ID: 3A54Download
MMDB ID: 83942
PDB Deposition Date: 2009/7/30
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 1.5  Å
Source Organism:
Similar Structures:
Biological Unit for 3A54: monomeric; determined by author and by software (PISA)
Molecular Components in 3A54
Label Count Molecule
Protein (1 molecule)
1
Protein-glutaminase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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