2H0F

Crystal Structure of PucM in the presence of 8-azaxanthine

2H0F の概要

• エントリーDOI: 10.2210/pdb2h0f/pdb
• 関連するPDBエントリー: 2H0E 2H0J
• 分子名称: Transthyretin-like protein pucM, 8-AZAXANTHINE (3 entities in total)
• 機能のキーワード: beta sandwitch, inhibitor complex, hiu, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27560.53

構造登録者

Rhee, S. (登録日: 2006-05-15, 公開日: 2006-06-27, 最終更新日: 2024-11-06)

主引用文献

Jung, D.-K.,Lee, Y.,Park, S.G.,Park, B.C.,Kim, G.-H.,Rhee, S.
Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family.
Proc.Natl.Acad.Sci.Usa, 103:9790-9795, 2006

PubMed Abstract: The ureide pathway, which produces ureides from uric acid, is an essential purine catabolic process for storing and transporting the nitrogen fixed in leguminous plants and some bacteria. PucM from Bacillus subtilis was recently characterized and found to catalyze the second reaction of the pathway, hydrolyzing 5-hydroxyisourate (HIU), a product of uricase in the first step. PucM has 121 amino acid residues and shows high sequence similarity to the functionally unrelated protein transthyretin (TTR), a thyroid hormone-binding protein. Therefore, PucM belongs to the TTR-related proteins (TRP) family. The crystal structures of PucM at 2.0 A and its complexes with the substrate analogs 8-azaxanthine and 5,6-diaminouracil reveal that even with their overall structure similarity, homotetrameric PucM and TTR are completely different, both in their electrostatic potential and in the size of the active sites located at the dimeric interface. Nevertheless, the absolutely conserved residues across the TRP family, including His-14, Arg-49, His-105, and the C-terminal Tyr-118-Arg-119-Gly-120-Ser-121, indeed form the active site of PucM. Based on the results of site-directed mutagenesis of these residues, we propose a possible mechanism for HIU hydrolysis. The PucM structure determined for the TRP family leads to the conclusion that diverse members of the TRP family would function similarly to PucM as HIU hydrolase.

PubMed: 16782815
DOI: 10.1073/pnas.0600523103

実験手法

X-RAY DIFFRACTION (2.7 Å)