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PDBsum entry 1jkf

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Isomerase PDB id
1jkf
Contents
Protein chains
466 a.a. *
Ligands
NAD ×2
Waters ×538
* Residue conservation analysis

References listed in PDB file
Key reference
Title The crystal structure and mechanism of 1-L-Myo-Inositol- 1-Phosphate synthase.
Authors A.J.Stein, J.H.Geiger.
Ref. J Biol Chem, 2002, 277, 9484-9491. [DOI no: 10.1074/jbc.M109371200]
PubMed id 11779862
Abstract
1-l-myo-Inositol-1-phosphate synthase catalyzes the conversion of d-glucose 6-phosphate to 1-l-myo-inositol-1-phosphate (MIP), the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. It involves an oxidation, intramolecular aldol cyclization, and reduction. We have determined the first crystal structure of MIP synthase. We present structures of both the NAD-bound enzyme and the enzyme bound to an inhibitor, 2-deoxy-glucitol-6-phosphate. While 58 amino acids are disordered in the unbound form of the enzyme in the vicinity of the active site, the inhibitor nucleates the folding of this domain in a striking example of induced fit, serving to completely encapsulate it within the enzyme. Three helices and a long beta-strand are formed in this process. We postulate a mechanism for the conversion based on the structure of the inhibitor-bound complex.
Figure 2.
Fig. 2. Ribbon model of the MIP synthase tetramer in the absence of inhibitor. This and all other structure figures were made using the program RIBBONS (55). The top two monomers are colored red and blue, make up one asymmetric unit, and are related by a noncrystallographic 2-fold axis that is roughly in the plane of the page. The bottom two monomers are green and are related to the top two monomers by a crystallographic 2-fold axis running roughly perpendicular to the page.
Figure 6.
Fig. 6. Proposed mechanism for the transformation catalyzed by MIP synthase.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 9484-9491) copyright 2002.
Secondary reference #1
Title Structural studies of mip synthase.
Authors A.J.Stein, J.H.Geiger.
Ref. Acta Crystallogr D Biol Crystallogr, 2000, 56, 348-350. [DOI no: 10.1107/S0907444999016777]
PubMed id 10713523
Full text Abstract
Figure 2.
Figure 2 Crystal images. (a) MIP synthase crystal form I. Note: crystal nucleated around a fiber. (b) MIP synthase crystal form II. (c) MIP synthase crystals produced via microseeding at a dilution of 10^-6.5.
The above figure is reproduced from the cited reference with permission from the IUCr
PROCHECK
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 Headers

 

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