5CC8

Structure of thiamine-monophosphate kinase from Acinetobacter baumannii in complex with AMPPNP

Summary for 5CC8

• Entry DOI: 10.2210/pdb5cc8/pdb
• Descriptor: Thiamine-monophosphate kinase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: ssgcid, structural genomics, seattle structural genomics center for infectious disease, transferase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 70105.50

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2015-07-01, release date: 2015-09-02, Last modification date: 2024-03-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)