5esx

<table><tr><td colspan='2'>[[5esx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_570-co-h Legionella pneumophila subsp. pneumophila 570-co-h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ESX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5esw|5esw]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lp12_1457 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=933093 Legionella pneumophila subsp. pneumophila 570-CO-H])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5esx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5esx OCA], [http://pdbe.org/5esx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5esx RCSB], [http://www.ebi.ac.uk/pdbsum/5esx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5esx ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

Crystal structures of Apo and GMP bound hypoxanthine-guanine phosphoribosyltransferase from Legionella pneumophila and the implications in gouty arthritis.,Zhang N, Gong X, Lu M, Chen X, Qin X, Ge H J Struct Biol. 2016 Jun;194(3):311-6. doi: 10.1016/j.jsb.2016.03.007. Epub 2016, Mar 8. PMID:26968365<ref>PMID:26968365</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 5esx" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Legionella pneumophila subsp. pneumophila 570-co-h]]

[[Category: Chen, X]]

[[Category: Ge, H]]

[[Category: Gong, X]]

[[Category: Lu, M]]

[[Category: Qin, X]]

[[Category: Zhang, N]]

[[Category: Transferase]]