2a7r
From Proteopedia
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|PDB= 2a7r |SIZE=350|CAPTION= <scene name='initialview01'>2a7r</scene>, resolution 3.00Å | |PDB= 2a7r |SIZE=350|CAPTION= <scene name='initialview01'>2a7r</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=5GP:GUANOSINE-5'-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7r OCA], [http://www.ebi.ac.uk/pdbsum/2a7r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a7r RCSB]</span> | ||
}} | }} | ||
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[[Category: Xie, Y.]] | [[Category: Xie, Y.]] | ||
[[Category: Zheng, M.]] | [[Category: Zheng, M.]] | ||
| - | [[Category: 5GP]] | ||
| - | [[Category: SO4]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:49:03 2008'' |
Revision as of 22:49, 30 March 2008
| |||||||
| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | GMP reductase, with EC number 1.7.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 01:49:03 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. | Oxidoreductase
