2a7r

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[[Image:2a7r.gif|left|200px]]
 
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==Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)==
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The line below this paragraph, containing "STRUCTURE_2a7r", creates the "Structure Box" on the page.
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<StructureSection load='2a7r' size='340' side='right'caption='[[2a7r]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2a7r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7R FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2a7r| PDB=2a7r | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7r OCA], [https://pdbe.org/2a7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7r RCSB], [https://www.ebi.ac.uk/pdbsum/2a7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7r ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)'''
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== Function ==
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[https://www.uniprot.org/uniprot/GMPR2_HUMAN GMPR2_HUMAN] Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation.<ref>PMID:12009299</ref> <ref>PMID:12669231</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/2a7r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a7r ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Guanosine monophosphate reductase (GMPR) catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP, and plays a critical role in re-utilization of free intracellular bases and purine nucleosides. Here, we report the first crystal structure of human GMP reductase 2 (hGMPR2) in complex with GMP at 3.0 A resolution. The protein forms a tetramer composed of subunits adopting the ubiquitous (alpha/beta)8 barrel fold. Interestingly, the substrate GMP is bound to hGMPR2 through interactions with Met269, Ser270, Arg286, Ser288, and Gly290; this makes the conformation of the adjacent flexible binding region (residues 268-289) fixed, much like a door on a hinge. Structure comparison and sequence alignment analyses show that the conformation of the active site loop (residues 179-187) is similar to those of hGMPR1 and inosine monophosphate dehydrogenases (IMPDHs). We propose that Cys186 is the potential active site, and that the conformation of the loop (residues 129-133) suggests a preference for the coenzyme NADPH over NADH. This structure provides important information towards understanding the functions of members of the GMPR family.
Guanosine monophosphate reductase (GMPR) catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP, and plays a critical role in re-utilization of free intracellular bases and purine nucleosides. Here, we report the first crystal structure of human GMP reductase 2 (hGMPR2) in complex with GMP at 3.0 A resolution. The protein forms a tetramer composed of subunits adopting the ubiquitous (alpha/beta)8 barrel fold. Interestingly, the substrate GMP is bound to hGMPR2 through interactions with Met269, Ser270, Arg286, Ser288, and Gly290; this makes the conformation of the adjacent flexible binding region (residues 268-289) fixed, much like a door on a hinge. Structure comparison and sequence alignment analyses show that the conformation of the active site loop (residues 179-187) is similar to those of hGMPR1 and inosine monophosphate dehydrogenases (IMPDHs). We propose that Cys186 is the potential active site, and that the conformation of the loop (residues 129-133) suggests a preference for the coenzyme NADPH over NADH. This structure provides important information towards understanding the functions of members of the GMPR family.
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==About this Structure==
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Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP.,Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y J Mol Biol. 2006 Feb 3;355(5):980-8. Epub 2005 Dec 1. PMID:16359702<ref>PMID:16359702</ref>
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2A7R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7R OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP., Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y, J Mol Biol. 2006 Feb 3;355(5):980-8. Epub 2005 Dec 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16359702 16359702]
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</div>
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[[Category: GMP reductase]]
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<div class="pdbe-citations 2a7r" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chen, F.]]
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[[Category: Chen F]]
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[[Category: Deng, Y.]]
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[[Category: Deng Y]]
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[[Category: Gong, W.]]
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[[Category: Gong W]]
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[[Category: Gu, X.]]
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[[Category: Gu X]]
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[[Category: Ji, C.]]
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[[Category: Ji C]]
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[[Category: Li, J.]]
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[[Category: Li J]]
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[[Category: Mao, Y.]]
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[[Category: Mao Y]]
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[[Category: Qiu, R.]]
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[[Category: Qiu R]]
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[[Category: Wei, Z.]]
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[[Category: Wei Z]]
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[[Category: Xie, Y.]]
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[[Category: Xie Y]]
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[[Category: Zheng, M.]]
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[[Category: Zheng M]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:42:57 2008''
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Current revision

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

PDB ID 2a7r

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