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3A55

Crystal structure of the A47Q2 mutant of pro- protein-glutaminase

Summary for 3A55
Entry DOI10.2210/pdb3a55/pdb
Related2ZK9 3A54 3A56
DescriptorProtein-glutaminase (2 entities in total)
Functional Keywordsmutant structure like the reaction intermediate, hydrolase
Biological sourceChryseobacterium proteolyticum
Total number of polymer chains2
Total formula weight67223.50
Authors
Hashizume, R.,Yamaguchi, S.,Mikami, B. (deposition date: 2009-07-30, release date: 2010-08-11, Last modification date: 2024-11-06)
Primary citationHashizume, 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: 21926168
DOI: 10.1074/jbc.M111.255133
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

239803

数据于2025-08-06公开中

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