2007
DOI: 10.1074/jbc.m700917200
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Crystal Structure of Human Cytosolic 5′-Nucleotidase II

Abstract: 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 adeninebased nucleotides and 2,3-bisphosphoglycerate. We have solved structures of cytosolic 5-nucleotidase II as native protein (2.2 Å ) and in complex with adenosine (1.5 Å ) and beryllium trifluoride (2.15 Å ). The … Show more

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Cited by 56 publications
(33 citation statements)
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“…The potential energy of the phosphonate nucleotides was minimized with a torsion force (set to 1000 kcal/mol) using Discover and the consistent valence force field in two phases, 1000 steps of steepest descent (SD) followed by 5000 steps of conjugate gradient with a tolerance of 0.001 kcal/mol Å (dielectric constant set to 1). The crystal structure of human cN-II [41] solved at high resolution (2JC9, 1.5 Å resolution) was used for docking of the various phosphonate analogues. A few new crystal structures of cN-II were solved since we have started our docking study, our choice to use 2JC9 was based on its better resolution and the absence of mutation in the active site (D52N) that could modify the interaction with the phosphonate group.…”
Section: Methodsmentioning
confidence: 99%
“…The potential energy of the phosphonate nucleotides was minimized with a torsion force (set to 1000 kcal/mol) using Discover and the consistent valence force field in two phases, 1000 steps of steepest descent (SD) followed by 5000 steps of conjugate gradient with a tolerance of 0.001 kcal/mol Å (dielectric constant set to 1). The crystal structure of human cN-II [41] solved at high resolution (2JC9, 1.5 Å resolution) was used for docking of the various phosphonate analogues. A few new crystal structures of cN-II were solved since we have started our docking study, our choice to use 2JC9 was based on its better resolution and the absence of mutation in the active site (D52N) that could modify the interaction with the phosphonate group.…”
Section: Methodsmentioning
confidence: 99%
“…Hs cN-IIIA (originally called pyrimidine-specific 5′-nucleotidase 1) catalyzes the hydrolysis of CMP and UMP [25]. Several crystal structures of cN-IIIA in complex with the substrate UMP [14] or representing different states of the reaction mechanism [10], [13] have been solved showing the molecular basis for substrate binding and catalysis. Superposition of the HAD core domains of cN-IIIA and cN-IIIB shows that the orientation of the cap domains with respect to the HAD core are slightly different ( Figure 6 ).…”
Section: Resultsmentioning
confidence: 99%
“…Five of them, namely cytosolic 5′-nucleotidase IA (cN-IA), cytosolic 5′-nucleotidase IB (cN-IB), cytosolic 5′-nucleotidase II (cN-II), cytosolic 5′-nucleotidase IIIA (cN-IIIA; previously called cN-III) and cytosolic 5′(3′)-deoxyribonucleotidase (cdN) are located in the cytosol whereas one is mitochondrial (mitochondrial-5′(3′)-deoxyribonucleotidase, mdN) and one is an extracellular enzyme (ecto-5′-nucleotidase, eN). Crystal structures are available for five of the seven nucleotidases including the mitochondrial (mdN) [5][7] and the extracellular nucleotidase (eN) [8], [9] as well as the cytosolic nucleotidases cdN [7], cN-II [10][12] and cN-IIIA [13], [14]. Although the intracellular 5′-nucleotidases generally share a low sequence similarity, all enzymes are magnesium-dependent and belong to the haloacid dehalogenase (HAD) superfamily [15].…”
Section: Introductionmentioning
confidence: 99%
“…dual activators/regulators, dual inhibitors/regulators, dual activators/inhibitors and multiple activators/inhibitors/regulators. For example, the endogenous theophylline can function as an allosteric activator for the adenosine receptor A1 (31) and as an allosteric inhibitor for the cAMP-specific 3′,5′-cyclic phosphodiesterase 4D (32); the endogenous ATP is involved in multiple allosteric regulation of targets, including cytosolic 5′-Nucleotidase II as an allosteric activator (33), glycogen phosphorylase α as an allosteric inhibitor (34) and aspartate carbamoyltransferase as an allosteric regulator (35). Due to the multiple targets of such modulators, there are 23 099 allosteric interactions between proteins and modulators recorded in ASD v2.0, larger than the total number of allosteric modulators.…”
Section: Expanded Database Contentsmentioning
confidence: 99%