5AK8

Structure of C351A mutant of Porphyromonas gingivalis peptidylarginine deiminase

Summary for 5AK8

• Entry DOI: 10.2210/pdb5ak8/pdb
• Related: 5AK7
• Descriptor: PEPTIDYLARGININE DEIMINASE, ALANINE, ARGININE, ... (6 entities in total)
• Functional Keywords: hydrolase, ppad
• Biological source: PORPHYROMONAS GINGIVALIS
• Total number of polymer chains: 1
• Total formula weight: 50311.16

Authors

Kopec, J.,Montgomery, A.,Shrestha, L.,Kiyani, W.,Nowak, R.,Burgess-Brown, N.,Venables, P.J.,Yue, W.W. (deposition date: 2015-03-02, release date: 2015-07-22, Last modification date: 2024-05-08)

Primary citation

Montgomery, A.B.,Kopec, J.,Shrestha, L.,Thezenas, M.L.,Burgess-Brown, N.A.,Fischer, R.,Yue, W.W.,Venables, P.J.
Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase: Implications for Autoimmunity in Rheumatoid Arthritis.
Ann.Rheum.Dis., 75:1255-, 2016

PubMed Abstract: Periodontitis (PD) is a known risk factor for rheumatoid arthritis (RA) and there is increasing evidence that the link between the two diseases is due to citrullination by the unique bacterial peptidylarginine deiminase (PAD) enzyme expressed by periodontal pathogen Pophyromonas gingivalis (PPAD). However, the precise mechanism by which PPAD could generate potentially immunogenic peptides has remained controversial due to lack of information about the structural and catalytic mechanisms of the enzyme.

PubMed: 26209657
DOI: 10.1136/ANNRHEUMDIS-2015-207656

Experimental method

X-RAY DIFFRACTION (1.48 Å)