1z2o: Difference between revisions

Revision as of 01:42, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z2o.png

Template:STRUCTURE 1z2o

Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with mg2+/ADP/Ins(1,3,4,6)P4Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with mg2+/ADP/Ins(1,3,4,6)P4

Template:ABSTRACT PUBMED 15837423

About this StructureAbout this Structure

1Z2O is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.

ReferenceReference

Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase., Miller GJ, Wilson MP, Majerus PW, Hurley JH, Mol Cell. 2005 Apr 15;18(2):201-12. PMID:15837423

Page seeded by OCA on Tue Jul 29 01:42:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1z2o.gif|left|200px]]
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 {{STRUCTURE_1z2o|  PDB=1z2o  |  SCENE=  }}
-'''Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with mg2+/ADP/Ins(1,3,4,6)P4'''
+===Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with mg2+/ADP/Ins(1,3,4,6)P4===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_15837423}}
 ==About this Structure==
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 [[Category: Atp-grasp]]
 [[Category: Inositol phosphate kinase]]
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