3OG9

Structure of YahD with Malic acid

Summary for 3OG9

• Entry DOI: 10.2210/pdb3og9/pdb
• Descriptor: protein yahD a copper inducible hydrolase, D-MALATE (3 entities in total)
• Functional Keywords: alpha/beta hydrolase, copper homeostasis, malic acid, hydrolase
• Biological source: Lactococcus lactis subsp. lactis (Streptococcus lactis)
• Total number of polymer chains: 2
• Total formula weight: 47445.48

Authors

Martinez Font, J.,Mancini, S.,Tauberger, E.,Moniot, S. (deposition date: 2010-08-16, release date: 2010-12-15, Last modification date: 2023-09-06)

Primary citation

Martinez, J.,Mancini, S.,Tauberger, E.,Weise, C.,Saenger, W.,Solioz, M.
Regulation and structure of YahD, a copper inducible alpha/beta hydrolase of Lactococcus lactis IL1403
Fems Microbiol.Lett., 314:57-66, 2011

PubMed Abstract: Lactococcus lactis IL1403 is a lactic acid bacterium that is used widely for food fermentation. Copper homeostasis in this organism chiefly involves copper secretion by the CopA copper ATPase. This enzyme is under the control of the CopR transcriptional regulator. CopR not only controls its own expression and that of CopA, but also that of an additional three operons and two monocistronic genes. One of the genes under the control of CopR, yahD, encodes an α/β-hydrolase. YahD expression was induced by copper and cadmium, but not by other metals or oxidative or nitrosative stress. The three-dimensional structure of YahD was determined by X-ray crystallography to a resolution of 1.88 Å. The protein was found to adopt an α/β-hydrolase fold with the characteristic Ser-His-Asp catalytic triad. Functional testing of YahD for a wide range of substrates for esterases, lipases, epoxide hydrolases, phospholipases, amidases and proteases was, however, unsuccessful. A copper-inducible serine hydrolase has not been described previously and YahD appears to be a new functional member of this enzyme family.

PubMed: 21059179
DOI: 10.1111/j.1574-6968.2010.02144.x

Experimental method

X-RAY DIFFRACTION (1.88 Å)