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New page: left|200px<br /> <applet load="2a7r" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a7r, resolution 3.00Å" /> '''Crystal structure o...
 
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[[Image:2a7r.gif|left|200px]]<br />
<applet load="2a7r" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2a7r, resolution 3.00&Aring;" />
'''Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)'''<br />


==Overview==
==Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)==
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.
<StructureSection load='2a7r' size='340' side='right'caption='[[2a7r]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/2a7r_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
2A7R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and 5GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/GMP_reductase GMP reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.7 1.7.1.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A7R OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16359702 16359702]
</div>
[[Category: GMP reductase]]
<div class="pdbe-citations 2a7r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chen, F.]]
[[Category: Chen F]]
[[Category: Deng, Y.]]
[[Category: Deng Y]]
[[Category: Gong, W.]]
[[Category: Gong W]]
[[Category: Gu, X.]]
[[Category: Gu X]]
[[Category: Ji, C.]]
[[Category: Ji C]]
[[Category: Li, J.]]
[[Category: Li J]]
[[Category: Mao, Y.]]
[[Category: Mao Y]]
[[Category: Qiu, R.]]
[[Category: Qiu R]]
[[Category: Wei, Z.]]
[[Category: Wei Z]]
[[Category: Xie, Y.]]
[[Category: Xie Y]]
[[Category: Zheng, M.]]
[[Category: Zheng M]]
[[Category: 5GP]]
[[Category: SO4]]
[[Category: oxidoreductase]]
 
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Retrieved from "https://proteopedia.org/2a7r"