2a7r

From Proteopedia

(Difference between revisions)

Revision as of 08:15, 15 May 2024

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

Structural highlights

2a7r is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y. NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol. 2002 Sep;34(9):1035-50. PMID:12009299
↑ Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X. Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells. J Cancer Res Clin Oncol. 2003 Feb;129(2):76-83. Epub 2003 Mar 1. PMID:12669231 doi:http://dx.doi.org/10.1007/s00432-002-0413-7
↑ Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y. Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP. J Mol Biol. 2006 Feb 3;355(5):980-8. Epub 2005 Dec 1. PMID:16359702 doi:10.1016/j.jmb.2005.11.047

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a7r"

@@ Line 3: / Line 3: @@
 <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/Human Human]. 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>
+<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='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>
+</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/GMP_reductase GMP reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.7 1.7.1.7] </span></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>
+[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]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: GMP reductase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[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: Oxidoreductase]]

2a7r

From Proteopedia

Revision as of 08:15, 15 May 2024

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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