2Z01

Crystal structure of phosphoribosylaminoimidazole synthetase from Geobacillus kaustophilus

2Z01 の概要

• エントリーDOI: 10.2210/pdb2z01/pdb
• 分子名称: Phosphoribosylformylglycinamidine cyclo-ligase (2 entities in total)
• 機能のキーワード: alpha and beta proteins, ligase, purine biosynthesis, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• 由来する生物種: Geobacillus kaustophilus
• 細胞内の位置: Cytoplasm : Q5L3D0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37045.73

構造登録者

Kanagawa, M.,Baba, S.,Kuramitsu, S.,Yokoyama, S.,Kawai, G.,Sampei, G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2007-05-06, 公開日: 2007-11-06, 最終更新日: 2023-10-25)

主引用文献

Kanagawa, M.,Baba, S.,Watanabe, Y.,Nakagawa, N.,Ebihara, A.,Kuramitsu, S.,Yokoyama, S.,Sampei, G.,Kawai, G.
Crystal structures and ligand binding of PurM proteins from Thermus thermophilus and Geobacillus kaustophilus
J.Biochem., 2015

PubMed Abstract: Crystal structures of 5-aminoimidazole ribonucleotide (AIR) synthetase, also known as PurM, from Thermus thermophilus (Tt) and Geobacillus kaustophilus (Gk) were determined. For TtPurM, the maximum resolution was 2.2 Å and the space group was P21212 with four dimers in an asymmetric unit. For GkPurM, the maximum resolution was 2.2 Å and the space group was P21212 with one monomer in asymmetric unit. The biological unit is dimer for both TtPurM and GkPurM and the dimer structures were similar to previously determined structures of PurM in general. For TtPurM, ∼50 residues at the amino terminal were disordered in the crystal structure whereas, for GkPurM, the corresponding region covered the ATP-binding site forming an α helix in part, suggesting that the N-terminal region of PurM changes its conformation upon binding of ligands. FGAM binding site was predicted by the docking simulation followed by the MD simulation based on the SO4 (2-) binding site found in the crystal structure of TtPurM.

PubMed: 26515187
DOI: 10.1093/jb/mvv107

実験手法

X-RAY DIFFRACTION (2.2 Å)