2j4e

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|PDB= 2j4e |SIZE=350|CAPTION= <scene name='initialview01'>2j4e</scene>, resolution 2.80&Aring;
|PDB= 2j4e |SIZE=350|CAPTION= <scene name='initialview01'>2j4e</scene>, resolution 2.80&Aring;
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+H'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+H'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ITT:INOSINE+5'-TRIPHOSPHATE'>ITT</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene> and <scene name='pdbligand=IMP:INOSINIC ACID'>IMP</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ITT:INOSINE+5&#39;-TRIPHOSPHATE'>ITT</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene> and <scene name='pdbligand=IMP:INOSINIC ACID'>IMP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Nucleoside-triphosphate_diphosphatase Nucleoside-triphosphate diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.19 3.6.1.19]
|ACTIVITY= [http://en.wikipedia.org/wiki/Nucleoside-triphosphate_diphosphatase Nucleoside-triphosphate diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.19 3.6.1.19]
|GENE=
|GENE=
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[[Category: nucleotide metabolism]]
[[Category: nucleotide metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:37:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:24:12 2008''

Revision as of 13:24, 23 March 2008

Image:2j4e.gif


PDB ID 2j4e

Drag the structure with the mouse to rotate
, resolution 2.80Å
Sites:
Ligands: , , and
Activity: Nucleoside-triphosphate diphosphatase, with EC number 3.6.1.19
Coordinates: save as pdb, mmCIF, xml



THE ITP COMPLEX OF HUMAN INOSINE TRIPHOSPHATASE


Contents

Overview

Inosine triphosphatase (ITPA) is a ubiquitous key regulator of cellular non-canonical nucleotide levels. It breaks down inosine and xanthine nucleotides generated by deamination of purine bases. Its enzymatic action prevents accumulation of ITP and reduces the risk of incorporation of potentially mutagenic inosine nucleotides into nucleic acids. Here we describe the crystal structure of human ITPA in complex with its prime substrate ITP, as well as the apoenzyme at 2.8 and 1.1A, respectively. These structures show for the first time the site of substrate and Mg2+ coordination as well as the conformational changes accompanying substrate binding in this class of enzymes. Enzyme substrate interactions induce an extensive closure of the nucleotide binding grove, resulting in tight interactions with the base that explain the high substrate specificity of ITPA for inosine and xanthine over the canonical nucleotides. One of the dimer contact sites is made up by a loop that is involved in coordinating the metal ion in the active site. We predict that the ITPA deficiency mutation P32T leads to a shift of this loop that results in a disturbed affinity for nucleotides and/or a reduced catalytic activity in both monomers of the physiological dimer.

Disease

Known disease associated with this structure: Inosine triphosphatase deficiency OMIM:[147520]

About this Structure

2J4E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T., Stenmark P, Kursula P, Flodin S, Graslund S, Landry R, Nordlund P, Schuler H, J Biol Chem. 2007 Feb 2;282(5):3182-7. Epub 2006 Nov 29. PMID:17138556

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