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New page: left|200px<br /><applet load="1jkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jkf, resolution 2.4Å" /> '''Holo 1L-myo-inositol-...
 
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[[Image:1jkf.gif|left|200px]]<br /><applet load="1jkf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jkf.gif|left|200px]]<br /><applet load="1jkf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jkf, resolution 2.4&Aring;" />
caption="1jkf, resolution 2.4&Aring;" />
'''Holo 1L-myo-inositol-1-phosphate Synthase'''<br />
'''Holo 1L-myo-inositol-1-phosphate Synthase'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1JKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-3-phosphate_synthase Inositol-3-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.4 5.5.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JKF OCA].  
1JKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-3-phosphate_synthase Inositol-3-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.4 5.5.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKF OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Geiger, J.H.]]
[[Category: Geiger, J H.]]
[[Category: Stein, A.J.]]
[[Category: Stein, A J.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: rossmann fold]]
[[Category: rossmann fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:20:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:36 2008''

Revision as of 11:23, 21 February 2008

File:1jkf.gif


1jkf, resolution 2.4Å

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Holo 1L-myo-inositol-1-phosphate Synthase

Overview

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.

About this Structure

1JKF is a Single protein structure of sequence from Saccharomyces cerevisiae with NAD as ligand. Active as Inositol-3-phosphate synthase, with EC number 5.5.1.4 Full crystallographic information is available from OCA.

Reference

The crystal structure and mechanism of 1-L-myo-inositol- 1-phosphate synthase., Stein AJ, Geiger JH, J Biol Chem. 2002 Mar 15;277(11):9484-91. Epub 2002 Jan 4. PMID:11779862

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