3GED

Fingerprint and Structural Analysis of a Apo SCOR enzyme from Clostridium thermocellum

「3DII」から置き換えられました

3GED の概要

• エントリーDOI: 10.2210/pdb3ged/pdb
• 関連するPDBエントリー: 3GEG
• 分子名称: Short-chain dehydrogenase/reductase SDR, GLYCEROL, THIOSULFATE, ... (5 entities in total)
• 機能のキーワード: sdr, scor, rossmann fold, oxidoreductase
• 由来する生物種: Clostridium thermocellum ATCC 27405
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55425.54

構造登録者

Huether, R.,Liu, Z.J.,Xu, H.,Wang, B.C.,Pletnev, V.,Mao, Q.,Umland, T.,Duax, W. (登録日: 2009-02-25, 公開日: 2009-03-17, 最終更新日: 2023-09-06)

主引用文献

Huether, R.,Liu, Z.J.,Xu, H.,Wang, B.C.,Pletnev, V.Z.,Mao, Q.,Duax, W.L.,Umland, T.C.
Sequence fingerprint and structural analysis of the SCOR enzyme A3DFK9 from Clostridium thermocellum.
Proteins, 78:603-613, 2010

PubMed Abstract: We have identified a highly conserved fingerprint of 40 residues in the TGYK subfamily of the short-chain oxidoreductase enzymes. The TGYK subfamily is defined by the presence of an N-terminal TGxxxGxG motif and a catalytic YxxxK motif. This subfamily contains more than 12,000 members, with individual members displaying unique substrate specificities. The 40 fingerprint residues are critical to catalysis, cofactor binding, protein folding, and oligomerization but are substrate independent. Their conservation provides critical insight into evolution of the folding and function of TGYK enzymes. Substrate specificity is determined by distinct combinations of residues in three flexible loops that make up the substrate-binding pocket. Here, we report the structure determinations of the TGYK enzyme A3DFK9 from Clostridium thermocellum in its apo form and with bound NAD(+) cofactor. The function of this protein is unknown, but our analysis of the substrate-binding loops putatively identifies A3DFK9 as a carbohydrate or polyalcohol metabolizing enzyme. C. thermocellum has potential commercial applications because of its ability to convert biomaterial into ethanol. A3DFK9 contains 31 of the 40 TGYK subfamily fingerprint residues. The most significant variations are the substitution of a cysteine (Cys84) for a highly conserved glycine within a characteristic VNNAG motif, and the substitution of a glycine (Gly106) for a highly conserved asparagine residue at a helical kink. Both of these variations occur at positions typically participating in the formation of a catalytically important proton transfer network. An alternate means of stabilizing this proton wire was observed in the A3DFK9 crystal structures.

PubMed: 19774618
DOI: 10.1002/prot.22584

実験手法

X-RAY DIFFRACTION (1.698 Å)