3OG9

Structure of YahD with Malic acid

3OG9 の概要

• エントリーDOI: 10.2210/pdb3og9/pdb
• 分子名称: protein yahD a copper inducible hydrolase, D-MALATE (3 entities in total)
• 機能のキーワード: alpha/beta hydrolase, copper homeostasis, malic acid, hydrolase
• 由来する生物種: Lactococcus lactis subsp. lactis (Streptococcus lactis)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47445.48

構造登録者

Martinez Font, J.,Mancini, S.,Tauberger, E.,Moniot, S. (登録日: 2010-08-16, 公開日: 2010-12-15, 最終更新日: 2023-09-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.88 Å)