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1dea

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[[Image:1dea.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION==
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|PDB= 1dea |SIZE=350|CAPTION= <scene name='initialview01'>1dea</scene>, resolution 2.1&Aring;
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<StructureSection load='1dea' size='340' side='right'caption='[[1dea]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1dea]] is a 2 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=1DEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEA FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] </span>
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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]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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|DOMAIN=
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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=1dea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dea OCA], [https://pdbe.org/1dea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dea RCSB], [https://www.ebi.ac.uk/pdbsum/1dea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dea ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dea OCA], [http://www.ebi.ac.uk/pdbsum/1dea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dea RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/NAGB_ECOLI NAGB_ECOLI] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.[HAMAP-Rule:MF_01241]
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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/de/1dea_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=1dea ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function. RESULTS: The crystal structure of glucosamine 6-phosphate deaminase with bound phosphate ions is presented at 2.1 A resolution together with the refined structures of the enzyme in complexes with its allosteric activator and with a competitive inhibitor. The protein fold can be described as a modified NAD-binding domain. CONCLUSIONS: From the similarities between the three presented structures, it is concluded that these represent the enzymatically active R state conformer. A mechanism for the deaminase reaction is proposed. It comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger.
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==About this Structure==
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1DEA 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=1DEA OCA].
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==Reference==
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Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution., Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E, Structure. 1995 Dec 15;3(12):1323-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8747459 8747459]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glucosamine-6-phosphate deaminase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Altamirano MM]]
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[[Category: Altamirano, M M.]]
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[[Category: Calcagno ML]]
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[[Category: Calcagno, M L.]]
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[[Category: Fontes MRM]]
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[[Category: Fontes, M R.M.]]
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[[Category: Garratt RC]]
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[[Category: Garratt, R C.]]
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[[Category: Horjales E]]
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[[Category: Horjales, E.]]
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[[Category: Oliva G]]
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[[Category: Oliva, G.]]
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[[Category: intramolecular oxidoreductase deaminase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:55 2008''
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Current revision

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

PDB ID 1dea

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