Summary for 2ZK9
| Entry DOI | 10.2210/pdb2zk9/pdb |
| Related | 3A54 3A55 3A56 |
| Descriptor | Protein-glutaminase, SODIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | deamidation glutaminase, hydrolase |
| Biological source | Chryseobacterium proteolyticum |
| Total number of polymer chains | 1 |
| Total formula weight | 19991.37 |
| Authors | Hashizume, R. (deposition date: 2008-03-13, release date: 2009-03-17, Last modification date: 2024-11-20) |
| Primary citation | Hashizume, R.,Maki, Y.,Mizutani, K.,Takahashi, N.,Matsubara, H.,Sugita, A.,Sato, K.,Yamaguchi, S.,Mikami, B. Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex J.Biol.Chem., 286:38691-38702, 2011 Cited by PubMed 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 Å 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 Å 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. PubMed: 21926168DOI: 10.1074/jbc.M111.255133 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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