1NRK

YGFZ PROTEIN

1NRK の概要

• エントリーDOI: 10.2210/pdb1nrk/pdb
• 分子名称: YGFZ Protein, SULFATE ION (3 entities in total)
• 機能のキーワード: ygfz, structural genomics, unknown function, structure 2 function project, s2f
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36947.25

構造登録者

Teplyakov, A.,Obmolova, G.,Gilliland, G.L.,Structure 2 Function Project (S2F) (登録日: 2003-01-24, 公開日: 2004-03-09, 最終更新日: 2024-11-20)

主引用文献

Teplyakov, A.,Obmolova, G.,Sarikaya, E.,Pullalarevu, S.,Krajewski, W.,Galkin, A.,Howard, A.J.,Herzberg, O.,Gilliland, G.L.
Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.
J.Bacteriol., 186:7134-7140, 2004

PubMed Abstract: The ygfZ gene product of Escherichia coli represents a large protein family conserved in bacteria to eukaryotes. The members of this family are uncharacterized proteins with marginal sequence similarity to the T-protein (aminomethyltransferase) of the glycine cleavage system. To assist with the functional assignment of the YgfZ family, the crystal structure of the E. coli protein was determined by multiwavelength anomalous diffraction. The protein molecule has a three-domain architecture with a central hydrophobic channel. The structure is very similar to that of bacterial dimethylglycine oxidase, an enzyme of the glycine betaine pathway and a homolog of the T-protein. Based on structural superposition, a folate-binding site was identified in the central channel of YgfZ, and the ability of YgfZ to bind folate derivatives was confirmed experimentally. However, in contrast to dimethylglycine oxidase and T-protein, the YgfZ family lacks amino acid conservation at the folate site, which implies that YgfZ is not an aminomethyltransferase but is likely a folate-dependent regulatory protein involved in one-carbon metabolism.

PubMed: 15489424
DOI: 10.1128/JB.186.21.7134-7140.2004

実験手法

X-RAY DIFFRACTION (2.8 Å)