1mor: Difference between revisions

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New page: left|200px<br /><applet load="1mor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mor, resolution 1.90Å" /> '''ISOMERASE DOMAIN OF ...
 
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'''ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATE'''<br />


==Overview==
==ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATE==
BACKGROUND: Glucosamine 6-phosphate synthase (GlmS) catalyses the first, step in hexosamine metabolism, converting fructose-6P (6 phosphate) into, glucosamine-6P using glutamine as a nitrogen source. GlmS is a bienzyme, complex consisting of two domains that catalyse glutamine hydrolysis and, sugar-phosphate isomerisation, respectively. Knowledge of the, three-dimensional structure of GlmS is essential for understanding the, general principles of catalysis by ketol isomerases and the mechanism of, nitrogen transfer in glutamine amidotransferases. RESULTS: The crystal, structure of the isomerase domain of the Escherichia coli GlmS with the, reaction product, glucosamine-6P, has been determined at 1.57 A, resolution. It is comprised of two topologically identical subdomains, each of which is dominated by a nucleotide-binding motif of a flavodoxin, type. The catalytic site is assembled by dimerisation of the protein., CONCLUSIONS: The isomerase active site of GlmS seems to be the result of, evolution through gene duplication and subsequent dimerisation., Isomerisation of fructose-6P is likely to involve the formation of a, Schiff base with Lys603 of the enzyme, the ring-opening step catalysed by, His504, and the proton transfer from C1 to C2 of the substrate effected by, Glu488. The highly conserved C-terminal fragment of the chain may play a, key role in substrate binding, catalysis and communication with the, glutaminase domain. The corresponding sequence pattern DXPXXLAK[SC]VT (in, single-letter amino-acid code, where X is any amino acid and letters in, brackets indicate that either serine or cysteine may take this position), may be considered as a fingerprint of GlmS.
<StructureSection load='1mor' size='340' side='right'caption='[[1mor]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mor]] is a 1 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=1MOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOR 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</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=1mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mor OCA], [https://pdbe.org/1mor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mor RCSB], [https://www.ebi.ac.uk/pdbsum/1mor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mor 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/mo/1mor_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=1mor ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MOR 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 G6P 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=1MOR OCA].
*[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]]
 
__TOC__
==Reference==
</StructureSection>
Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain., Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Polikarpov I, Structure. 1998 Aug 15;6(8):1047-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9739095 9739095]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Teplyakov A]]
[[Category: Teplyakov, A.]]
[[Category: G6P]]
[[Category: glutamine amidotransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:35:34 2007''

Latest revision as of 10:46, 14 February 2024

ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATEISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATE

Structural highlights

1mor is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLMS_ECOLI Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

Evolutionary Conservation

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

See Also

1mor, resolution 1.90Å

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