Bifunctional purine biosynthesis protein PURH

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== Function ==
== Function ==
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Bifunctional purine biosynthesis protein PURH (PURH) is a bifunctional enzyme which catalyzes the last two steps in purine biosynthesis. PURH is composed of 2 functionally independent domains linked by a flexible domain. The N-terminal domain possesses IMP cyclohydrolase activity (see also [[Cyclohydrolase]]) and the C-terminal domain possesses aminoimidazole 4-carboxamide ribonucleotide transformylase activity<ref>PMID:22139174</ref>.
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'''Bifunctional purine biosynthesis protein PURH''' (PURH) is a bifunctional enzyme which catalyzes the last two steps in purine biosynthesis. PURH is composed of 2 functionally independent domains linked by a flexible domain. The N-terminal domain possesses IMP cyclohydrolase activity (see also [[Cyclohydrolase]]) and the C-terminal domain possesses aminoimidazole 4-carboxamide ribonucleotide transformylase activity<ref>PMID:22139174</ref>.
Aminoimidazole 4-carboxamide-4-carboxylic acid (AICAR) is an allosteric activator of AMP-activated protein kinase.
Aminoimidazole 4-carboxamide-4-carboxylic acid (AICAR) is an allosteric activator of AMP-activated protein kinase.
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== Structural highlights ==
== Structural highlights ==
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The 3D structure of human PURH shows the <scene name='84/842877/Cv/4'>XMP nucleotide bound in the IMP cyclohydrolase domain</scene> and the <scene name='84/842877/Cv/9'>activator AICAR and the inhibitor bound at the interface of dimer making numerous interactions with both PHRH monomers</scene><ref>PMID:14966129</ref>. Water molecules are shown as red spheres.
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The 3D structure of human PURH shows the <scene name='84/842877/Cv/10'>XMP nucleotide bound in the IMP cyclohydrolase domain</scene> and the <scene name='84/842877/Cv/11'>activator AICAR and the inhibitor bound at the interface of dimer making numerous interactions with both PHRH monomers</scene><ref>PMID:14966129</ref>. Water molecules are shown as red spheres.
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Current revision

Human PURH dimer complex with activator AICAR, XMP, inhibitor and K+ ion (purple) (PDB code 1p4r)

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3D structures of bifunctional purine biosynthesis protein PURH

Updated on 30-May-2024

1pkx - hPURH + XMP - human
5uy8, 5uz0 - hPURH + AICAR + inhibitor
1p4r, 1pl0 - hPURH + AICAR + XMP + inhibitor
1oz0 - cPURH - chicken
1thz, 2iu3, 2iu0, 2b1g, 2b1i - cPURH + inhibitor
1m9n - cPURH + AICAR + XMP
1zcz - PURH - Thermotoga maritima
3zzm - MtPURH + CFAIR - Mycobacterium tuberculosis
4a1o - MtPURH + AICAR + CFAIR
2ntm - MetPURH - Methanothermobacter thermautotrophicus
2ntl - MetPURH + AICAR
2ntk - MetPURH + IMP

References

  1. ↑ Qiu X, Yuan Y, Gao Y. Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1590-4., doi: 10.1107/S1744309111039960. Epub 2011 Nov 26. PMID:22139174 doi:http://dx.doi.org/10.1107/S1744309111039960
  2. ↑ McGuire JJ. Anticancer antifolates: current status and future directions. Curr Pharm Des. 2003;9(31):2593-613. doi: 10.2174/1381612033453712. PMID:14529544 doi:http://dx.doi.org/10.2174/1381612033453712
  3. ↑ Cheong CG, Wolan DW, Greasley SE, Horton PA, Beardsley GP, Wilson IA. Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates. J Biol Chem. 2004 Apr 23;279(17):18034-45. Epub 2004 Feb 13. PMID:14966129 doi:10.1074/jbc.M313691200

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