6LK4

Crystal structure of GMP reductase from Trypanosoma brucei in complex with guanosine 5'-triphosphate

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6LK4 の概要

• エントリーDOI: 10.2210/pdb6lk4/pdb
• 分子名称: Guanosine 5'-monophosphate Reductase, GUANOSINE-5'-TRIPHOSPHATE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: trypanosoma brucei, 5'-monophosphate reductase, guanosine 5'-triphosphate, cystathionine beta synthase motif, oxidoreductase
• 由来する生物種: Trypanosoma brucei brucei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54456.39

構造登録者

Mase, H.,Otani, T.,Imamura, A.,Nishimura, S.,Inui, T. (登録日: 2019-12-18, 公開日: 2020-03-18, 最終更新日: 2023-11-22)

主引用文献

Imamura, A.,Okada, T.,Mase, H.,Otani, T.,Kobayashi, T.,Tamura, M.,Kubata, B.K.,Inoue, K.,Rambo, R.P.,Uchiyama, S.,Ishii, K.,Nishimura, S.,Inui, T.
Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.
Nat Commun, 11:1837-1837, 2020

PubMed Abstract: Guanosine 5'-monophosphate reductase (GMPR) is involved in the purine salvage pathway and is conserved throughout evolution. Nonetheless, the GMPR of Trypanosoma brucei (TbGMPR) includes a unique structure known as the cystathionine-β-synthase (CBS) domain, though the role of this domain is not fully understood. Here, we show that guanine and adenine nucleotides exert positive and negative effects, respectively, on TbGMPR activity by binding allosterically to the CBS domain. The present structural analyses revealed that TbGMPR forms an octamer that shows a transition between relaxed and twisted conformations in the absence and presence of guanine nucleotides, respectively, whereas the TbGMPR octamer dissociates into two tetramers when ATP is available instead of guanine nucleotides. These findings demonstrate that the CBS domain plays a key role in the allosteric regulation of TbGMPR by facilitating the transition of its oligomeric state depending on ligand nucleotide availability.

PubMed: 32296055
DOI: 10.1038/s41467-020-15611-3

実験手法

X-RAY DIFFRACTION (2.503 Å)