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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"
caption="1jkf, resolution 2.4&Aring;" />
'''Holo 1L-myo-inositol-1-phosphate Synthase'''<br />


==Overview==
==Holo 1L-myo-inositol-1-phosphate Synthase==
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.
<StructureSection load='1jkf' size='340' side='right'caption='[[1jkf]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jkf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JKF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jkf OCA], [https://pdbe.org/1jkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jkf RCSB], [https://www.ebi.ac.uk/pdbsum/1jkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jkf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/INO1_YEAST INO1_YEAST]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jk/1jkf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jkf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:11779862</ref>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11779862 11779862]
</div>
[[Category: Inositol-3-phosphate synthase]]
<div class="pdbe-citations 1jkf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Geiger JH]]
[[Category: Geiger, J.H.]]
[[Category: Stein AJ]]
[[Category: Stein, A.J.]]
[[Category: NAD]]
[[Category: rossmann fold]]
 
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Latest revision as of 09:37, 25 December 2024

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

1jkf, resolution 2.40Å

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