2jc9: Difference between revisions

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[[Category: polymorphism]]
[[Category: polymorphism]]


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Revision as of 18:25, 30 October 2007

File:2jc9.gif


2jc9, resolution 1.50Å

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CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC 5'-NUCLEOTIDASE II IN COMPLEX WITH ADENOSINE

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 ... [(full description)]

About this StructureAbout this Structure

2JC9 is a [Single protein] structure of sequence from [Homo sapiens] with MG, SO4, ADN and GOL as [ligands]. Active as [5'-nucleotidase], with EC number [3.1.3.5]. Structure known Active Site: AC1. 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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