Structural highlights
Function
COAW_STAAS Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.[1]
Publication Abstract from PubMed
Pantothenate kinase (PanK) is the rate-limiting enzyme in Coenzyme A biosynthesis, catalyzing the ATP-dependent phosphorylation of pantothenate. We solved the co-crystal structures of PanKs from Staphylococcus aureus (SaPanK) and Klebsiella pneumonia (KpPanK) with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide (N354-Pan). Two different N354-Pan conformers interact with polar/nonpolar mixed residues in SaPanK and aromatic residues in KpPanK. Additionally, phosphorylated N354-Pan is found at the closed active site of SaPanK but not at the open active site of KpPanK, suggesting an exchange of the phosphorylated product with a new N354-Pan only in KpPanK. Together, pantothenamides conformational flexibility and binding pocket are two key considerations for selective compound design. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumonia and Staphylococcus aureus.,Hughes SJ, Antoshchenko T, Kim KP, Smil D, Park HW Proteins. 2014 Jan 28. doi: 10.1002/prot.24524. PMID:24470271[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hong BS, Yun MK, Zhang YM, Chohnan S, Rock CO, White SW, Jackowski S, Park HW, Leonardi R. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Structure. 2006 Aug;14(8):1251-61. PMID:16905099 doi:10.1016/j.str.2006.06.008
- ↑ Hughes SJ, Antoshchenko T, Kim KP, Smil D, Park HW. Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumonia and Staphylococcus aureus. Proteins. 2014 Jan 28. doi: 10.1002/prot.24524. PMID:24470271 doi:http://dx.doi.org/10.1002/prot.24524
