4AQK

Inositol 1,3,4,5,6-pentakisphosphate 2-kinase in complex with ADP and IP6

Summary for 4AQK

• Entry DOI: 10.2210/pdb4aqk/pdb
• Related: 2XAL 2XAM 2XAN 2XAO 2XAR
• Descriptor: INOSITOL-PENTAKISPHOSPHATE 2-KINASE, INOSITOL HEXAKISPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: transferase, inositide kinase, phytic acid, inositide signalling, insp5 2-k
• Biological source: ARABIDOPSIS THALIANA (THALE CRESS)
• Total number of polymer chains: 1
• Total formula weight: 52498.16

Authors

I Banos-Sanz, J.,Sanz-Aparicio, J.,Gonzalez, B. (deposition date: 2012-04-18, release date: 2012-05-02, Last modification date: 2023-12-20)

Primary citation

Banos-Sanz, J.I.,Sanz-Aparicio, J.,Brearley, C.A.,Gonzalez, B.
Expression, Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of the Apo Form of Insp5 2-K from Arabidopsis Thaliana.
Acta Crystallogr.,Sect.F, 68:701-, 2012

PubMed Abstract: Inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IP(5) 2-K) is a key enzyme that catalyzes the synthesis of phytic acid (IP(6)) from inositol 1,3,4,5,6-pentakisphosphate (IP(5)) and ATP. The first structure of IP(5) 2-K, that from Arabidopsis thaliana, has been solved previously; it only crystallized in the presence of inositol, either the substrate IP(5) or the product IP(6), and failed to crystallize in its free state (without inositol). Based on structural analysis, a point mutation of IP(5) 2-K (W129A) has been produced in order to overcome this limitation and obtain information about protein conformational changes upon substrate binding. Here, the production and crystallization of W129A IP(5) 2-K in its free state and with bound nucleotide is described. These crystals differed from the native crystals and belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 66.00, b = 68.23, c = 105.80 Å and a = 63.06, b = 71.80, c = 100.23 Å, respectively. The crystals diffracted to resolutions of 2.22 Å (apo) and 2.05 Å (nucleotide bound) using synchrotron radiation and contained one molecule per asymmetric unit. The structures have been determined using the molecular-replacement method and refinement is being undertaken.

PubMed: 22684075
DOI: 10.1107/S1744309112017307

Experimental method

X-RAY DIFFRACTION (2.4 Å)