1rm0: Difference between revisions

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New page: left|200px<br /><applet load="1rm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rm0, resolution 2.05Å" /> '''Crystal Structure of...
 
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[[Image:1rm0.gif|left|200px]]<br /><applet load="1rm0" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate'''<br />


==Overview==
==Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate==
1l-myo-inositol 1-phosphate (MIP) synthase catalyzes the conversion of, d-glucose 6-phosphate to 1l-myo-inositol 1-phosphate, the first and, rate-limiting step in the biosynthesis of all inositol-containing, compounds. It involves an oxidation, enolization, intramolecular aldol, cyclization, and reduction. Here we present the structure of MIP synthase, in complex with NAD(+) and a high-affinity inhibitor, 2-deoxy-d-glucitol, 6-(E)-vinylhomophosphonate. This structure reveals interactions between, the enzyme active site residues and the inhibitor that are significantly, different from that proposed for 2-deoxy-d-glucitol 6-phosphate in the, previously published structure of MIP synthase-NAD(+)-2-deoxy-d-glucitol, 6-phosphate. There are several other conformational changes in NAD(+) and, the enzyme active site as well. Based on the new structural data, we, propose a new and completely different mechanism for MIP synthase.
<StructureSection load='1rm0' size='340' side='right'caption='[[1rm0]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1rm0]] 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=1RM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RM0 FirstGlance]. <br>
1RM0 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 MN, D6P and NAI as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1RM0 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D6P:(3,4,5,7-TETRAHYDROXY-HEPT-1-ENYL)-PHOSPHONIC+ACID'>D6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm0 OCA], [https://pdbe.org/1rm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1rm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rm0 ProSAT]</span></td></tr>
The structure of the 1L-myo-inositol-1-phosphate synthase-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism., Jin X, Foley KM, Geiger JH, J Biol Chem. 2004 Apr 2;279(14):13889-95. Epub 2003 Dec 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14684747 14684747]
</table>
[[Category: Inositol-3-phosphate synthase]]
== 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/rm/1rm0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1rm0 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Foley KM]]
[[Category: Foley, K.M.]]
[[Category: Geiger JH]]
[[Category: Geiger, J.H.]]
[[Category: Jin X]]
[[Category: Jin, X.]]
[[Category: D6P]]
[[Category: MN]]
[[Category: NAI]]
[[Category: myo-inositol 1-phosphate synthase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:42:09 2007''

Latest revision as of 11:24, 14 February 2024

Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonateCrystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate

Structural highlights

1rm0 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

INO1_YEAST

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1rm0, resolution 2.05Å

Drag the structure with the mouse to rotate

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OCA
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