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

Zhang, N.,Gong, X.,Lu, M.,Chen, X.,Qin, X.,Ge, H. (deposition date: 2015-11-17, release date: 2016-03-30, Last modification date: 2023-11-08)

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

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: 26968365
DOI: 10.1016/j.jsb.2016.03.007

Experimental method

X-RAY DIFFRACTION (2.4 Å)