2vkq
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2vkq.jpg|left|200px]] | + | [[Image:2vkq.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE III (CN-III, NT5C3) IN COMPLEX WITH BERYLLIUM TRIFLUORIDE''' | + | {{Structure |
| + | |PDB= 2vkq |SIZE=350|CAPTION= <scene name='initialview01'>2vkq</scene>, resolution 2.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Bef+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Mg+Binding+Site+For+Chain+A'>AC2</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=BEF:BERYLLIUM TRIFLUORIDE ION'>BEF</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE III (CN-III, NT5C3) IN COMPLEX WITH BERYLLIUM TRIFLUORIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2VKQ is a [ | + | 2VKQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17405878 17405878] |
[[Category: 5'-nucleotidase]] | [[Category: 5'-nucleotidase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 59: | Line 68: | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:47:26 2008'' |
Revision as of 16:47, 20 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | and | ||||||
| Activity: | 5'-nucleotidase, with EC number 3.1.3.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE III (CN-III, NT5C3) IN COMPLEX WITH BERYLLIUM TRIFLUORIDE
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
2VKQ 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 Thu Mar 20 18:47:26 2008
Categories: 5'-nucleotidase | Homo sapiens | Single protein | Arrowsmith, C H. | Berg | Berglund, H. | Busam, R. | Collins, R. | Dahlgren, L G. | Den | Edwards, A. | Flodin, S. | Flores, A. | Graslund, S. | Hammarstrom, M. | Herman, M D. | Johansson, A. | Johansson, I. | Kallas, A. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nilsson, M E. | Nordlund, P. | Nyman, T. | Persson, C. | Sagemark, J. | Sgc, Structural GenomicsConsortium. | Thorsell, A G. | Tresaugues, L. | Van, S. | Wallden, K. | Weigelt, J. | Welin, M. | BEF | MG | Alternative splicing | Cytoplasm | Disease mutation | Endoplasmic reticulum | Hemolytic anemia | Hydrolase | Nucleotidase | Nucleotide metabolism | Nucleotide-binding | Phosphotransferase
