2FCJ

Structure of small TOPRIM domain protein from Bacillus stearothermophilus.

2FCJ の概要

• エントリーDOI: 10.2210/pdb2fcj/pdb
• 分子名称: small TOPRIM domain protein, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: toprim domain, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 41727.73

構造登録者

Rezacova, P.,Chen, Y.,Borek, D.,Collart, F.,Joachimiak, A.,Otwinowski, Z.,Midwest Center for Structural Genomics (MCSG) (登録日: 2005-12-12, 公開日: 2006-01-24, 最終更新日: 2024-12-25)

主引用文献

Rezacova, P.,Borek, D.,Moy, S.F.,Joachimiak, A.,Otwinowski, Z.
Crystal structure and putative function of small Toprim domain-containing protein from Bacillus stearothermophilus.
Proteins, 70:311-319, 2008

PubMed Abstract: The crystal structure of the Midwest Center for Structural Genomics target APC35832, a 14.7-kDa cytosolic protein from Bacillus stearothermophilus, has been determined at 1.3 A resolution by the single anomalous diffraction method from a mercury soaked crystal. The APC35832 protein is a representative of large group of bacterial and archeal proteins entirely consisting of the Toprim (topoisomerase-primase) domain. This domain is found in the catalytic centers of many enzymes catalyzing phosphodiester bond formation or cleavage, but the function of small Toprim domain proteins remains unknown. Consistent with the sequence analysis, the APC35832 structure shows a conserved Toprim fold, with a central 4-stranded parallel beta-sheet surrounded by four alpha-helixes. Comparison of the APC35832 structure with its closest structural homolog, the catalytic core of bacteriophage T7 primase, revealed structural conservation of a metal binding site and isothermal titration calorimetry indicates that APC35832 binds Mg2+ with a sub-millimolar dissociation constant (K(d)). The APC35832-Mg2+ complex structure was determined at 1.65 A and reveals the role of conserved acidic residues in Mg2+ ion coordination. The structural similarities to other Toprim domain containing proteins and potential function and substrates of APC35832 are discussed in this article.

PubMed: 17705269
DOI: 10.1002/prot.21511

実験手法

X-RAY DIFFRACTION (1.3 Å)