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New page: left|200px<br /><applet load="1jxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxa, resolution 3.1Å" /> '''GLUCOSAMINE 6-PHOSPHA...
 
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[[Image:1jxa.gif|left|200px]]<br /><applet load="1jxa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jxa, resolution 3.1&Aring;" />
'''GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE'''<br />


==Overview==
==GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE==
Glucosamine-6-phosphate synthase catalyses the first and rate-limiting, step in hexosamine metabolism, converting fructose 6-phosphate into, glucosamine 6-phosphate in the presence of glutamine. The crystal, structure of the Escherichia coli enzyme reveals the domain organisation, of the homodimeric molecule. The 18 A hydrophobic channel sequestered from, the solvent connects the glutaminase and isomerase active sites, and, provides a means of ammonia transfer from glutamine to sugar phosphate., The C-terminal decapeptide sandwiched between the two domains plays a, central role in the transfer. Based on the structure, a mechanism of, enzyme action and self-regulation is proposed. It involves large domain, movements triggered by substrate binding that lead to the formation of the, channel.
<StructureSection load='1jxa' size='340' side='right'caption='[[1jxa]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jxa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JXA 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</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=1jxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jxa OCA], [https://pdbe.org/1jxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jxa RCSB], [https://www.ebi.ac.uk/pdbsum/1jxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jxa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLMS_ECOLI GLMS_ECOLI] Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
== 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/jx/1jxa_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=1jxa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.


==About this Structure==
Channeling of ammonia in glucosamine-6-phosphate synthase.,Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:11700065<ref>PMID:11700065</ref>
1JXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with G6Q as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JXA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Channeling of ammonia in glucosamine-6-phosphate synthase., Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA, J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11700065 11700065]
</div>
<div class="pdbe-citations 1jxa" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Badet B]]
[[Category: Badet, B.]]
[[Category: Badet-Denisot MA]]
[[Category: Badet-Denisot, M.A.]]
[[Category: Obmolova G]]
[[Category: Obmolova, G.]]
[[Category: Teplyakov A]]
[[Category: Teplyakov, A.]]
[[Category: G6Q]]
[[Category: ammonia channel]]
[[Category: beta-sandwich]]
[[Category: gene duplication]]
[[Category: nucleotide-binding fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:39:33 2007''

Latest revision as of 09:37, 25 December 2024

GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE

1jxa, resolution 3.10Å

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