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| - | [[Image:1mor.gif|left|200px]] | |
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| - | {{Structure
| + | ==ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATE== |
| - | |PDB= 1mor |SIZE=350|CAPTION= <scene name='initialview01'>1mor</scene>, resolution 1.90Å
| + | <StructureSection load='1mor' size='340' side='right'caption='[[1mor]], [[Resolution|resolution]] 1.90Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>
| + | <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> |
| - | |ACTIVITY= <span class='plainlinks'>[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] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | |GENE=
| + | <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> |
| - | |DOMAIN=
| + | <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> |
| - | |RELATEDENTRY= | + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mor OCA], [http://www.ebi.ac.uk/pdbsum/1mor PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mor RCSB]</span>
| + | == 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> |
| | | | |
| - | '''ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATE'''
| + | ==See Also== |
| - | | + | *[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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==
| + | |
| - | 1MOR is a [[Single protein]] structure of sequence from [http://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].
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| - | | + | |
| - | ==Reference==
| + | |
| - | 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://www.ncbi.nlm.nih.gov/pubmed/9739095 9739095]
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| | [[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: glutamine amidotransferase]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:58 2008''
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