Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4Y04

Crystal structure of dipeptidyl peptidase 11 (DPP11) from Porphyromonas gingivalis (Space)

Summary for 4Y04
Entry DOI10.2210/pdb4y04/pdb
Related4XZY 4Y01 4Y02 4Y06
DescriptorPeptidase S46, POTASSIUM ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsspace, wt, hydrolase
Biological sourcePorphyromonas gingivalis
Total number of polymer chains1
Total formula weight82216.49
Authors
Sakamoto, Y.,Suzuki, Y.,Iizuka, I.,Tateoka, C.,Roppongi, S.,Fujimoto, M.,Inaka, K.,Tanaka, H.,Yamada, M.,Ohta, K.,Nonaka, T.,Ogasawara, W.,Tanaka, N. (deposition date: 2015-02-05, release date: 2015-07-15, Last modification date: 2024-10-30)
Primary citationSakamoto, Y.,Suzuki, Y.,Iizuka, I.,Tateoka, C.,Roppongi, S.,Fujimoto, M.,Inaka, K.,Tanaka, H.,Yamada, M.,Ohta, K.,Gouda, H.,Nonaka, T.,Ogasawara, W.,Tanaka, N.
Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.
Sci Rep, 5:11151-11151, 2015
Cited by
PubMed Abstract: The dipeptidyl peptidase 11 from Porphyromonas gingivalis (PgDPP11) belongs to the S46 family of serine peptidases and preferentially cleaves substrates with Asp/Glu at the P1 position. The molecular mechanism underlying the substrate specificity of PgDPP11, however, is unknown. Here, we report the crystal structure of PgDPP11. The enzyme contains a catalytic domain with a typical double β-barrel fold and a recently identified regulatory α-helical domain. Crystal structure analyses, docking studies, and biochemical studies revealed that the side chain of Arg673 in the S1 subsite is essential for recognition of the Asp/Glu side chain at the P1 position of the bound substrate. Because S46 peptidases are not found in mammals and the Arg673 is conserved among DPP11s, we anticipate that DPP11s could be utilised as targets for antibiotics. In addition, the present structure analyses could be useful templates for the design of specific inhibitors of DPP11s from pathogenic organisms.
PubMed: 26057589
DOI: 10.1038/srep11151
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.66 Å)
Structure validation

238268

数据于2025-07-02公开中

PDB statisticsPDBj update infoContact PDBjnumon