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1moq

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(New page: 200px<br /><applet load="1moq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1moq, resolution 1.57&Aring;" /> '''ISOMERASE DOMAIN OF ...)
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[[Image:1moq.jpg|left|200px]]<br /><applet load="1moq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1moq, resolution 1.57&Aring;" />
 
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'''ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE'''<br />
 
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==Overview==
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==ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE==
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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.
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<StructureSection load='1moq' size='340' side='right'caption='[[1moq]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1moq]] 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=1MOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOQ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1moq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1moq OCA], [https://pdbe.org/1moq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1moq RCSB], [https://www.ebi.ac.uk/pdbsum/1moq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1moq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1moq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1moq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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:9739095<ref>PMID:9739095</ref>
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1MOQ 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 GLP, SO4, NA, MES and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1MOQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1moq" style="background-color:#fffaf0;"></div>
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[[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]]
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[[Category: Single protein]]
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[[Category: Teplyakov, A.]]
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[[Category: GLP]]
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[[Category: MES]]
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[[Category: MRD]]
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[[Category: NA]]
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[[Category: SO4]]
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[[Category: glutamine amidotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:35:30 2007''
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==See Also==
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*[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Teplyakov A]]

Current revision

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

PDB ID 1moq

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