2a7r

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|PDB= 2a7r |SIZE=350|CAPTION= <scene name='initialview01'>2a7r</scene>, resolution 3.00&Aring;
|PDB= 2a7r |SIZE=350|CAPTION= <scene name='initialview01'>2a7r</scene>, resolution 3.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=5GP:GUANOSINE-5'-MONOPHOSPHATE'>5GP</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=5GP:GUANOSINE-5&#39;-MONOPHOSPHATE'>5GP</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= [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]
|GENE=
|GENE=
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:46:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:35:19 2008''

Revision as of 12:35, 23 March 2008

Image:2a7r.gif


PDB ID 2a7r

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands: and
Activity: GMP reductase, with EC number 1.7.1.7
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

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