Bifunctional purine biosynthesis protein PURH

spinqualitylabelsall models Human PURH dimer complex with activator AICAR, XMP, inhibitor and K+ ion (purple) (PDB code 1p4r) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function 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. Aminoimidazole 4-carboxamide-4-carboxylic acid (AICAR) is an allosteric activator of AMP-activated protein kinase. Relevance Purine biosynthesis anti-folate inhibitors, amongst them PURH inhibitors, are widely used as anti-cancer therapy. Structural highlights The 3D structure of human PURH shows the XMP nucleotide bound in the IMP cyclohydrolase domain and the activator AICAR and the inhibitor bound at the interface of dimer making numerous interactions with both PHRH monomers. Water molecules are shown as red spheres.

3D structures of bifunctional purine biosynthesis protein PURH

Updated on 30-May-2024

Cyclohydrolase - 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

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