Pantothenate kinase

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(New page: '''Pantothenate kinase''' (PanK) phosphorylates pantothenate (vitamin B5) (PAU) to form 4’-phosphopantothenate (PPT) using ATP as phosphate source. This is the first step in coenzyme A...)
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<StructureSection load='' size='350' side='right' caption='Pantothenate kinase III dimer complex with pantothenate, glycerol and ethane diol, [[2f9w]]' scene='52/525168/Cv/1' pspeed='8'>
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'''Pantothenate kinase''' (PanK) phosphorylates pantothenate (vitamin B5) (PAU) to form 4’-phosphopantothenate (PPT) using ATP as phosphate source. This is the first step in coenzyme A biosynthesis. PanK is regulated by feedback inhibition by CoA and its thioesters. Three types of PanK are known. PanK I found in bacteria; PanK II found mostly in eukaryotes; PanK III found in bacteria and known as CoaX.
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== Function ==
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'''Pantothenate kinase''' (PanK) phosphorylates pantothenate (vitamin B5) (PAU) to form 4’-phosphopantothenate (PPT) using ATP as phosphate source. This is the first step in coenzyme A biosynthesis<ref>. PanK is regulated by feedback inhibition by CoA and its thioesters.PMID:9890959</ref>.<br />
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==3D structures of pantothenate kinase==
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Three types of PanK are known.<br >
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* '''PanK I''' found in bacteria<br />
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* '''PanK II''' found mostly in eukaryotes<br />
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* '''PanK III''' found in bacteria and known as CoaX.
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[[1esm]] – EcPanK + CoA – ''Escherichia coli''<br />
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== Disease ==
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[[1esn]] - EcPanK + ANP<br />
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Mutations in PanK II cause the autosomal-recessive disorder Pantothenate kinase-associated neurodegeneration<ref>PMID:15911822</ref>.
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[[1sq5]] - EcPanK + ADP + PAU<br />
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[[3tqc]] - PanK – ''Coxiella burnetii''
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==PanK I binary complex==
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== Structural highlights ==
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<scene name='52/525168/Cv/5'>Pantothenate binds in a buried pocket at the PanK dimer interface</scene><ref>PMID:16905099</ref>.
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*<scene name='52/525168/Cv/6'>Buried pocket at the PanK dimer interface</scene>.
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[[2ges]], [[2get]], [[2zs7]], [[2geu]], [[2gev]] - MtPanK + CoA derivative – ''Mycobacterium tuberculosis''<br />
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==3D structures of pantothenate kinase==
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[[2zs8]], [[2zsb]] - MtPanK + ADP<br />
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[[Pantothenate kinase 3D structures]]
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[[3af1]] - MtPanK + GDP <br />
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[[3af2]] - MtPanK + AMPPCP<br />
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[[3af4]] - MtPanK + GMPPCP<br />
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[[2zsd]] - MtPanK + CoA<br />
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[[3avo]] - MtPanK + PAU<br />
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[[3avp]], [[3avq]] - MtPanK + PAU derivative
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==PanK I ternary complex==
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[[2zs9]] - MtPanK + ADP + PAU<br />
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[[2zse]] - MtPanK + AMPPCP + PAU<br />
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[[3af3]] - MtPanK + GMPPCP + PAU<br />
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[[2zsf]] - MtPanK + ADP + ATP<br />
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[[2zsa]] - MtPanK + ADP + PPT<BR />
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[[3aez]] - MtPanK + GDP + PPT<BR />
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[[3af0]] - MtPanK + GDP + PAU<br />
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===PanK II===
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[[2ews]] - PanK + ANP – ''Staphylococcus aureus''
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===PanK III===
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[[2gtd]] - TmPanK – ''Thermotoga maritima''<br />
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[[2f9t]] – PaPanK – ''Pseudomonas aeruginosa''<br />
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[[2h3g]] - PanK – ''Bacillus anthracis''<br />
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[[3djc]] - PanK – ''Legionella pneumophila''<br />
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==PanK III binary complex==
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[[2f9w]] - PaPanK + PAU<br />
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[[3bex]] - TmPanK + PAU<br />
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[[3bf3]] - TmPanK + PPT<BR />
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==PanK III ternary complex==
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[[3bf1]] - TmPanK + ADP + PAU<br />
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===Human PanK===
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</StructureSection>
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[[2i7n]], [[3smp]] - hPanK 1 α + CoA - human<br />
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== References ==
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[[2i7p]], [[3mk6]] - hPanK 3 + CoA<br />
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<references/>
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[[3sms]] – hPanK 3 + PAU analog
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[[Category:Topic Page]]

Current revision

Pantothenate kinase III dimer complex with pantothenate, glycerol and ethane diol, 2f9w

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References

  1. ↑ . PanK is regulated by feedback inhibition by CoA and its thioesters.PMID:9890959
  2. ↑ Pellecchia MT, Valente EM, Cif L, Salvi S, Albanese A, Scarano V, Bonuccelli U, Bentivoglio AR, D'Amico A, Marelli C, Di Giorgio A, Coubes P, Barone P, Dallapiccola B. The diverse phenotype and genotype of pantothenate kinase-associated neurodegeneration. Neurology. 2005 May 24;64(10):1810-2. PMID:15911822 doi:http://dx.doi.org/10.1212/01.WNL.0000161843.52641.EC
  3. ↑ 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

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