3S2Z

Crystal structure of the Lactobacillus johnsonii cinnamoyl esterase LJ0536 S106A mutant in complex with caffeic acid

Summary for 3S2Z

• Entry DOI: 10.2210/pdb3s2z/pdb
• Related: 3PF8 3PF9 3PFB 3PFC
• Descriptor: Cinnamoyl esterase, CHLORIDE ION, CAFFEIC ACID, ... (4 entities in total)
• Functional Keywords: alpha/beta hydrolase fold, esterase, hydrolase, cinnamoyl/feruloyl esterase, hydroxycinammates
• Biological source: Lactobacillus johnsonii
• Total number of polymer chains: 2
• Total formula weight: 60948.57

Authors

Stogios, P.J.,Lai, K.K.,Vu, C.,Xu, X.,Cui, H.,Molloy, S.,Gonzalez, C.F.,Yakunin, A.,Savchenko, A. (deposition date: 2011-05-17, release date: 2011-08-31, Last modification date: 2023-09-13)

Primary citation

Lai, K.K.,Stogios, P.J.,Vu, C.,Xu, X.,Cui, H.,Molloy, S.,Savchenko, A.,Yakunin, A.,Gonzalez, C.F.
An inserted alpha/beta subdomain shapes the catalytic pocket of Lactobacillus johnsonii cinnamoyl esterase.
Plos One, 6:e23269-e23269, 2011

PubMed Abstract: Microbial enzymes produced in the gastrointestinal tract are primarily responsible for the release and biochemical transformation of absorbable bioactive monophenols. In the present work we described the crystal structure of LJ0536, a serine cinnamoyl esterase produced by the probiotic bacterium Lactobacillus johnsonii N6.2.

PubMed: 21876742
DOI: 10.1371/journal.pone.0023269

Experimental method

X-RAY DIFFRACTION (1.76 Å)