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2j6h
From Proteopedia
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| - | [[Image:2j6h.gif|left|200px]]<br /> | ||
| - | <applet load="2j6h" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2j6h, resolution 2.35Å" /> | ||
| - | '''E. COLI GLUCOSAMINE-6-P SYNTHASE IN COMPLEX WITH GLUCOSE-6P AND 5-OXO-L-NORLEUCINE'''<br /> | ||
| - | == | + | ==E. coli glucosamine-6-P synthase in complex with glucose-6P and 5-oxo- L-norleucine== |
| - | Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from | + | <StructureSection load='2j6h' size='340' side='right'caption='[[2j6h]], [[Resolution|resolution]] 2.35Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2j6h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bpj 2bpj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J6H 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]] 2.35Å</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>, <scene name='pdbligand=ONL:5-OXO-L-NORLEUCINE'>ONL</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=2j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6h OCA], [https://pdbe.org/2j6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j6h RCSB], [https://www.ebi.ac.uk/pdbsum/2j6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j6h 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/j6/2j6h_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=2j6h ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from fructose-6P and glutamine and uses a channel to transfer ammonia from its glutaminase to its synthase active site. X-ray structures of glucosamine-6P synthase have been determined at 2.05 Angstroms resolution in the presence of fructose-6P and at 2.35 Angstroms resolution in the presence of fructose-6P and 6-diazo-5-oxo-L-norleucine, a glutamine affinity analog that covalently modifies the N-terminal catalytic cysteine, therefore mimicking the gamma-glutamyl-thioester intermediate formed during hydrolysis of glutamine. The fixation of the glutamine analog activates the enzyme through several major structural changes: 1) the closure of a loop to shield the glutaminase site accompanied by significant domain hinging, 2) the activation of catalytic residues involved in glutamine hydrolysis, i.e. the alpha-amino group of Cys-1 and Asn-98 that is positioned to form the oxyanion hole, and 3) a 75 degrees rotation of the Trp-74 indole group that opens the ammonia channel. | ||
| - | + | Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase.,Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:16339762<ref>PMID:16339762</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2j6h" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Golinelli-Pimpaneau B]] | ||
| + | [[Category: Mouilleron S]] | ||
Current revision
E. coli glucosamine-6-P synthase in complex with glucose-6P and 5-oxo- L-norleucine
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