2j2c

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[[Image:2j2c.jpg|left|200px]]
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{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] </span>
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{{STRUCTURE_2j2c| PDB=2j2c | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j2c OCA], [http://www.ebi.ac.uk/pdbsum/2j2c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j2c RCSB]</span>
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'''CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE II (NT5C2, CN-II)'''
'''CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE II (NT5C2, CN-II)'''
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[[Category: Weigelt, J.]]
[[Category: Weigelt, J.]]
[[Category: Welin, M.]]
[[Category: Welin, M.]]
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[[Category: allosteric enzyme]]
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[[Category: Allosteric enzyme]]
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[[Category: cn-ii]]
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[[Category: Cn-ii]]
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[[Category: cytosolic 5-prime nucleotidase ii]]
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[[Category: Cytosolic 5-prime nucleotidase ii]]
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[[Category: cytosolic purine 5-prime nucleotidase]]
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[[Category: Cytosolic purine 5-prime nucleotidase]]
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[[Category: gmp-imp specific nucleotidase]]
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[[Category: Gmp-imp specific nucleotidase]]
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[[Category: high km 5-prime nucleotidase]]
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[[Category: High km 5-prime nucleotidase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: nt5c2]]
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[[Category: Nt5c2]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:02 2008''
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Revision as of 05:14, 4 May 2008

Template:STRUCTURE 2j2c

CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE II (NT5C2, CN-II)


Overview

Cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates and regulates the IMP and GMP pools within the cell. It possesses phosphotransferase activity and thereby also catalyzes the reverse reaction. Both reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. We have solved structures of cytosolic 5'-nucleotidase II as native protein (2.2 Angstrom) and in complex with adenosine (1.5 Angstrom) and beryllium trifluoride (2.15 Angstrom) The tetrameric enzyme is structurally similar to enzymes of the haloacid dehalogenase (HAD) superfamily, including mitochondrial 5'(3')-deoxyribonucleotidase and cytosolic 5'-nucleotidase III but possesses additional regulatory regions that contain two allosteric effector sites. At effector site 1 located near a subunit interface we modeled diadenosine tetraphosphate with one adenosine moiety in each subunit. This efficiently glues the tetramer subunits together in pairs. The model shows why diadenosine tetraphosphate but not diadenosine triphosphate activates the enzyme and supports a role for cN-II during apoptosis when the level of diadenosine tetraphosphate increases. We have also modeled 2,3-bisphosphoglycerate in effector site 1 using one phosphate site from each subunit. By comparing the structure of cytosolic 5'-nucleotidase II with that of mitochondrial 5'(3')-deoxyribonucleotidase in complex with dGMP, we identified residues involved in substrate recognition.

About this Structure

2J2C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition., Wallden K, Stenmark P, Nyman T, Flodin S, Graslund S, Loppnau P, Bianchi V, Nordlund P, J Biol Chem. 2007 Jun 15;282(24):17828-36. Epub 2007 Apr 3. PMID:17405878 Page seeded by OCA on Sun May 4 08:14:50 2008

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