4MB0

Crystal structure of TON1374

Summary for 4MB0

• Entry DOI: 10.2210/pdb4mb0/pdb
• Related: 4MB2
• Descriptor: phosphopantothenate synthetase, ACETATE ION (3 entities in total)
• Functional Keywords: ligase
• Biological source: Thermococcus onnurineus
• Total number of polymer chains: 4
• Total formula weight: 118989.04

Authors

Kim, M.-K.,An, Y.J.,Cha, S.-S. (deposition date: 2013-08-19, release date: 2014-08-06, Last modification date: 2024-03-20)

Primary citation

Kim, M.-K.,An, Y.J.,Cha, S.-S.
The crystal structure of a novel phosphopantothenate synthetase from the hyperthermophilic archaea, Thermococcus onnurineus NA1
Biochem.Biophys.Res.Commun., 439:533-538, 2013

PubMed Abstract: Pantothenate is the essential precursor of coenzyme A (CoA), a fundamental cofactor in all aspects of metabolism. In bacteria and eukaryotes, pantothenate synthetase (PS) catalyzes the last step in the pantothenate biosynthetic pathway, and pantothenate kinase (PanK) phosphorylates pantothenate for its entry into the CoA biosynthetic pathway. However, genes encoding PS and PanK have not been identified in archaeal genomes. Recently, a comparative genomic analysis and the identification and characterization of two novel archaea-specific enzymes show that archaeal pantoate kinase (PoK) and phosphopantothenate synthetase (PPS) represent counterparts to the PS/PanK pathway in bacteria and eukaryotes. The TON1374 protein from Thermococcus onnurineus NA1 is a PPS, that shares 54% sequence identity with the first reported archaeal PPS candidate, MM2281, from Methanosarcina mazei and 91% sequence identity with TK1686, the PPS from Thermococcus kodakarensis. Here, we report the apo and ATP-complex structures of TON1374 and discuss the substrate-binding mode and reaction mechanism.

PubMed: 24021277
DOI: 10.1016/j.bbrc.2013.09.008

Experimental method

X-RAY DIFFRACTION (1.96 Å)