2a7r
From Proteopedia
(New page: 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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caption="2a7r, resolution 3.00Å" /> | caption="2a7r, resolution 3.00Å" /> | ||
'''Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)'''<br /> | '''Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Guanosine monophosphate reductase (GMPR) catalyzes the irreversible and | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=5GP:'>5GP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:26 2008'' |
Revision as of 14:24, 21 February 2008
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Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)
Overview
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
2A7R is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as GMP reductase, with EC number 1.7.1.7 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:24:26 2008
Categories: GMP reductase | Homo sapiens | Single protein | Chen, F. | Deng, Y. | Gong, W. | Gu, X. | Ji, C. | Li, J. | Mao, Y. | Qiu, R. | Wei, Z. | Xie, Y. | Zheng, M. | 5GP | SO4 | Oxidoreductase
