2j2c: Difference between revisions

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==About this Structure==
==About this Structure==
2J2C 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>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J2C OCA].  
2J2C 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>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J2C OCA].  


==Reference==
==Reference==
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[[Category: polymorphism]]
[[Category: polymorphism]]


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Revision as of 11:40, 3 February 2008

File:2j2c.jpg


2j2c, resolution 2.20Å

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

OverviewOverview

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 StructureAbout this Structure

2J2C is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as 5'-nucleotidase, with EC number 3.1.3.5 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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

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