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| {{STRUCTURE_1z2n| PDB=1z2n | SCENE= }} | | {{STRUCTURE_1z2n| PDB=1z2n | SCENE= }} |
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| '''Inositol 1,3,4-trisphosphate 5/6-kinase complexed Mg2+/ADP'''
| | ===Inositol 1,3,4-trisphosphate 5/6-kinase complexed Mg2+/ADP=== |
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| ==Overview==
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| Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15837423}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15837423 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15837423}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Atp-grasp]] | | [[Category: Atp-grasp]] |
| [[Category: Inositol phosphate kinase]] | | [[Category: Inositol phosphate kinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:06:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:48:18 2008'' |
