5ESW
Crystal structure of Apo hypoxanthine-guanine phosphoribosyltransferase from Legionella pneumophila
Summary for 5ESW
Entry DOI | 10.2210/pdb5esw/pdb |
Related | 5ESX |
Descriptor | Purine/pyrimidine phosphoribosyltransferase, PHOSPHATE ION (3 entities in total) |
Functional Keywords | hypoxanthine-guanine phosphoribosyltransferase, transferase |
Biological source | Legionella pneumophila subsp. pneumophila strain Philadelphia 1 |
Total number of polymer chains | 2 |
Total formula weight | 44231.76 |
Authors | |
Primary citation | Zhang, N.,Gong, X.,Lu, M.,Chen, X.,Qin, X.,Ge, H. Crystal structures of Apo and GMP bound hypoxanthine-guanine phosphoribosyltransferase from Legionella pneumophila and the implications in gouty arthritis J.Struct.Biol., 194:311-316, 2016 Cited by PubMed Abstract: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (EC 2.4.2.8) reversibly catalyzes the transfer of the 5-phophoribosyl group from 5-phosphoribosyl-alpha-1-pyrophosphate (PRPP) to hypoxanthine or guanine to form inosine monophosphate (IMP) or guanosine monophosphate (GMP) in the purine salvage pathway. To investigate the catalytic mechanism of this enzyme in the intracellular pathogen Legionella pneumophila, we determined the crystal structures of the L. pneumophila HGPRT (LpHGPRT) both in its apo-form and in complex with GMP. The structures reveal that LpHGPRT comprises a core domain and a hood domain which are packed together to create a cavity for GMP-binding and the enzymatic catalysis. The binding of GMP induces conformational changes of the stable loop II. This new binding site is closely related to the Gout arthritis-linked human HGPRT mutation site (Ser103Arg). Finally, these structures of LpHGPRT provide insights into the catalytic mechanism of HGPRT. PubMed: 26968365DOI: 10.1016/j.jsb.2016.03.007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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