5CM7

Structure of thiamine-monophosphate kinase from Acinetobacter baumannii in complex with adenosine diphosphate (ADP) and thiamine diphosphate (TPP)

5CM7 の概要

• エントリーDOI: 10.2210/pdb5cm7/pdb
• 分子名称: Thiamine-monophosphate kinase, ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: ssgcid, acinetobacter baumannii, thiamine-monophosphate kinase, thiamine diphosphate, tpp, adenosine diphosphate, adp, structural genomics, seattle structural genomics center for infectious disease, transferase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70808.68

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2015-07-16, 公開日: 2015-08-26, 最終更新日: 2023-09-27)

主引用文献

Sullivan, A.H.,Dranow, D.M.,Horanyi, P.S.,Lorimer, D.D.,Edwards, T.E.,Abendroth, J.
Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.
Sci Rep, 9:4392-4392, 2019

PubMed Abstract: Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen A. baumanii in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.

PubMed: 30867460
DOI: 10.1038/s41598-019-40558-x

実験手法

X-RAY DIFFRACTION (1.55 Å)