4E8G

Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound mg

4E8G の概要

• エントリーDOI: 10.2210/pdb4e8g/pdb
• 分子名称: Mandelate racemase/muconate lactonizing enzyme, N-terminal domain protein, MAGNESIUM ION, UNKNOWN LIGAND, ... (4 entities in total)
• 機能のキーワード: putative racemase, nysgrc, structural genomics, psi-biology, new york structural genomics research consortium, isomerase
• 由来する生物種: Paracoccus denitrificans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84698.81

構造登録者

Vetting, M.W.,Toro, R.,Bhosle, R.,Wasserman, S.R.,Morisco, L.L.,Sojitra, S.,Chamala, S.,Kar, A.,Lafleur, J.,Villigas, G.,Evans, B.,Hammonds, J.,Gizzi, A.,Zencheck, W.D.,Hillerich, B.,Love, J.,Seidel, R.D.,Bonanno, J.B.,Gerlt, J.A.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC) (登録日: 2012-03-20, 公開日: 2012-05-02, 最終更新日: 2024-10-09)

主引用文献

Kumar, R.,Zhao, S.,Vetting, M.W.,Wood, B.M.,Sakai, A.,Cho, K.,Solbiati, J.,Almo, S.C.,Sweedler, J.V.,Jacobson, M.P.,Gerlt, J.A.,Cronan, J.E.
Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine.
MBio, 5:e00933-e00913, 2014

PubMed Abstract: Through the use of genetic, enzymatic, metabolomic, and structural analyses, we have discovered the catabolic pathway for proline betaine, an osmoprotectant, in Paracoccus denitrificans and Rhodobacter sphaeroides. Genetic and enzymatic analyses showed that several of the key enzymes of the hydroxyproline betaine degradation pathway also function in proline betaine degradation. Metabolomic analyses detected each of the metabolic intermediates of the pathway. The proline betaine catabolic pathway was repressed by osmotic stress and cold stress, and a regulatory transcription factor was identified. We also report crystal structure complexes of the P. denitrificans HpbD hydroxyproline betaine epimerase/proline betaine racemase with l-proline betaine and cis-hydroxyproline betaine.

PubMed: 24520058
DOI: 10.1128/mBio.00933-13

実験手法

X-RAY DIFFRACTION (2 Å)