5dd7

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

spinqualitylabelsall models 5dd7, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dd7 is a 2 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: ANP, EDO, K, MG, TPS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0D5YC82_ACIBA Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.[HAMAP-Rule:MF_02128] Publication Abstract from PubMed 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. Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.,Sullivan AH, Dranow DM, Horanyi PS, Lorimer DD, Edwards TE, Abendroth J Sci Rep. 2019 Mar 13;9(1):4392. doi: 10.1038/s41598-019-40558-x. PMID:30867460 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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