8JT1

COLLAGENASE FROM GRIMONTIA (VIBRIO) HOLLISAE 1706B COMPLEXED WITH GLY-PRO-HYP-GLY-PRO-HYP

Summary for 8JT1

• Entry DOI: 10.2210/pdb8jt1/pdb
• Descriptor: Microbial collagenase, 6-mer peptide, ZINC ION, ... (9 entities in total)
• Functional Keywords: grimontia hollisae, collagenase, hydrolase
• Biological source: Grimontia hollisae; More
• Total number of polymer chains: 8
• Total formula weight: 133472.34

Authors

Ueshima, S.,Yaskawa, K.,Takita, T.,Mikami, B. (deposition date: 2023-06-21, release date: 2024-02-07)

Primary citation

Ueshima, S.,Yasumoto, M.,Kitagawa, Y.,Akazawa, K.,Takita, T.,Tanaka, K.,Hattori, S.,Mizutani, K.,Mikami, B.,Yasukawa, K.
Insights into the catalytic mechanism of Grimontia hollisae collagenase through structural and mutational analyses.
Febs Lett., 597:2473-2483, 2023

PubMed Abstract: Grimontia hollisae collagenase (Ghcol) exhibits high collagen-degrading activity. To explore its catalytic mechanism, its substrate (Gly-Pro-Hyp-Gly-Pro-Hyp, GPOGPO)-complexed crystal structure was determined at 2.0 Å resolution. A water molecule was observed near the active-site zinc ion. Since this water was not observed in the product (GPO)-complexed Ghcol, it was hypothesized that the GPOGPO-complexed Ghcol structure reflects a Michaelis complex, providing a structural basis for understanding the catalytic mechanism. Analyses of the active-site geometry and site-directed mutagenesis of the active-site tyrosine residues revealed that Glu493 and Tyr564 were essential for catalysis, suggesting that Glu493 functions as an acid and base catalyst while Tyr564 stabilizes the tetrahedral complex in the transition state. These results shed light on the catalytic mechanism of bacterial collagenase.

PubMed: 37698340
DOI: 10.1002/1873-3468.14732

Experimental method

X-RAY DIFFRACTION (2 Å)