Pantothenate kinase: Difference between revisions

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</StructureSection>
</StructureSection>
==3D structures of pantothenate kinase==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*'''PanK I'''
**[[1esm]] – EcPanK + CoA – ''Escherichia coli''<br />
**[[1esn]] - EcPanK + ANP<br />
**[[1sq5]] - EcPanK + ADP + PAU<br />
**[[3tqc]] - PanK – ''Coxiella burnetii''<br />
**[[5xlv]] - MtPanK – ''Mycobacterium tuberculosis''<br />
**[[5xlw]], [[5xmb]] - MtPanK (mutant)<br />
*PanK I binary complex
**[[2ges]], [[2get]], [[2zs7]], [[2geu]], [[2gev]] - MtPanK + CoA derivative <br />
**[[2zs8]], [[2zsb]] - MtPanK + ADP<br />
**[[3af1]] - MtPanK + GDP <br />
**[[3af2]] - MtPanK + AMPPCP<br />
**[[3af4]] - MtPanK + GMPPCP<br />
**[[2zsd]] - MtPanK + CoA<br />
**[[3avo]] - MtPanK + PAU<br />
**[[3avp]], [[3avq]] - MtPanK + PAU derivative<br />
**[[4bfs]], [[4bft]], [[4bfu]], [[4bfv]], [[4bfw]], [[4bfx]] - MtPanK + triazole inhibitor<br />
**[[4bfy]], [[4bfz]] - MtPanK + biaryl inhibitor<br />
*PanK I ternary complex
**[[2zs9]] - MtPanK + ADP + PAU<br />
**[[2zse]] - MtPanK + AMPPCP + PAU<br />
**[[3af3]] - MtPanK + GMPPCP + PAU<br />
**[[2zsf]] - MtPanK + ADP + ATP<br />
**[[2zsa]] - MtPanK + ADP + PPT<BR />
**[[3aez]] - MtPanK + GDP + PPT<BR />
**[[3af0]] - MtPanK + GDP + PAU<br />
**[[4f7w]], [[4ne2]] – KpPanK + ADP + pantothenamide derivative – ''Klebsiella pneumonia''<br />
**[[4gi7]] – KpPanK + ADP + pantothenate analog<br />
*'''PanK II'''
**[[2ews]] - SaPanK + ANP – ''Staphylococcus aureus''<br />
**[[4nb4]], [[4m7x]], [[4m7y]], [[5elz]], [[5jic]], [[6avp]], [[6awi]], [[6awj]], [[6ebv]] - SaPanK + ADP + pantothenate derivative<br />
**[[6awh]] - SaPanK + ATP + pantothenate derivative<br />
**[[6awg]] - SaPanK + ADP + ATP + pantothenate derivative<br />
*'''PanK III'''
**[[2gtd]] - TmPanK – ''Thermotoga maritima''<br />
**[[2f9t]] – PaPanK – ''Pseudomonas aeruginosa''<br />
**[[2h3g]] - PanK – ''Bacillus anthracis''<br />
**[[3djc]] - PanK – ''Legionella pneumophila''<br />
**[[4o8k]] - BtPanK – ''Burkholderia thailandensis''<br />
*PanK III binary complex
**[[2f9w]] - PaPanK + PAU<br />
**[[3bex]] - TmPanK + PAU<br />
**[[3bf3]] - TmPanK + PPT<BR />
*PanK III higher complexes
**[[3bf1]] - TmPanK + ADP + PAU<br />
**[[4o5f]] - BtPanK + ADP + PAU <br />
**[[5b8h]] - BtPanK + ADP + PAU + imidodiphosphate<br />
*'''Human PanK'''
**[[2i7n]], [[3smp]] - hPanK 1 α + CoA - human<br />
**[[5e26]] - hPanK 2 + ADP + PAU <br />
**[[2i7p]], [[3mk6]] - hPanK 3 + CoA<br />
**[[3sms]] – hPanK 3 + PAU analog<br />
**[[5kpt]] - hPanK 3 + AMPPNP  <br />
**[[5kq8]] - hPanK 3 + AMPPN <br />
**[[5kpr]] - hPanK 3 + AMPPNP + PAU <br />
**[[5kpz]] - hPanK 3 + ADP + PAU <br />
**[[5kqd]] - hPanK 3 + palmitoyl-CoA <br />
**[[6b3v]] - hPanK 3 + ANP + drug <br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:09, 13 November 2019


Function

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[1].

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.

Disease

Mutations in PanK II cause the autosomal-recessive disorder Pantothenate kinase-associated neurodegeneration[2].

Structural highlights

[3].

  • .

3D structures of pantothenate kinase

Pantothenate kinase 3D structures


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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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Michal Harel, Alexander Berchansky, Joel L. Sussman