1cd5

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[[Image:1cd5.jpg|left|200px]]
 
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==GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER==
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The line below this paragraph, containing "STRUCTURE_1cd5", creates the "Structure Box" on the page.
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<StructureSection load='1cd5' size='340' side='right'caption='[[1cd5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1cd5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CD5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.3&#8491;</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=1cd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cd5 OCA], [https://pdbe.org/1cd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cd5 RCSB], [https://www.ebi.ac.uk/pdbsum/1cd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cd5 ProSAT]</span></td></tr>
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{{STRUCTURE_1cd5| PDB=1cd5 | SCENE= }}
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</table>
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== Function ==
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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/cd/1cd5_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=1cd5 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: The allosteric hexameric enzyme glucosamine-6-phosphate deaminase from Escherichia coli catalyses the regulatory step of N-acetylglucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia. The reversibility of the catalysis and its rapid-equilibrium random kinetic mechanism, among other properties, make this enzyme a good model for studying allosteric processes. RESULTS: Here we present the structure of P6(3)22 crystals, obtained in sodium acetate, of GlcN6P deaminase in its ligand-free T state. These crystals are very sensitive to X-ray radiation and have a high (78%) solvent content. The activesite lid (residues 162-185) is highly disordered in the T conformer; this may contribute significantly to the free-energy change of the whole allosteric transition. Comparison of the structure with the crystallographic coordinates of the R conformer (Brookhaven Protein Data Bank entry 1 dea) allows us to describe the geometrical changes associated with the allosteric transition as the movement of two rigid entities within each monomer. The active site, located in a deep cleft between these two rigid entities, presents a more open geometry in the T conformer than in the R conformer. CONCLUSIONS: The differences in active-site geometry are related to alterations in the substrate-binding properties associated with the allosteric transition. The rigid nature of the two mobile structural units of each monomer seems to be essential in order to explain the observed kinetics of the deaminase hexamer. The triggers for both the homotropic and heterotropic allosteric transitions are discussed and particular residues are assigned to these functions. A structural basis for an entropic term in the allosteric transition is an interesting new feature that emerges from this study.
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'''GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER'''
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The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution.,Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G Structure. 1999 May;7(5):527-37. PMID:10378272<ref>PMID:10378272</ref>
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==Overview==
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BACKGROUND: The allosteric hexameric enzyme glucosamine-6-phosphate deaminase from Escherichia coli catalyses the regulatory step of N-acetylglucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia. The reversibility of the catalysis and its rapid-equilibrium random kinetic mechanism, among other properties, make this enzyme a good model for studying allosteric processes. RESULTS: Here we present the structure of P6(3)22 crystals, obtained in sodium acetate, of GlcN6P deaminase in its ligand-free T state. These crystals are very sensitive to X-ray radiation and have a high (78%) solvent content. The activesite lid (residues 162-185) is highly disordered in the T conformer; this may contribute significantly to the free-energy change of the whole allosteric transition. Comparison of the structure with the crystallographic coordinates of the R conformer (Brookhaven Protein Data Bank entry 1 dea) allows us to describe the geometrical changes associated with the allosteric transition as the movement of two rigid entities within each monomer. The active site, located in a deep cleft between these two rigid entities, presents a more open geometry in the T conformer than in the R conformer. CONCLUSIONS: The differences in active-site geometry are related to alterations in the substrate-binding properties associated with the allosteric transition. The rigid nature of the two mobile structural units of each monomer seems to be essential in order to explain the observed kinetics of the deaminase hexamer. The triggers for both the homotropic and heterotropic allosteric transitions are discussed and particular residues are assigned to these functions. A structural basis for an entropic term in the allosteric transition is an interesting new feature that emerges from this study.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1CD5 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=1CD5 OCA].
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</div>
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<div class="pdbe-citations 1cd5" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution., Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G, Structure. 1999 May;7(5):527-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10378272 10378272]
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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[[Category: Escherichia coli]]
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== References ==
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[[Category: Glucosamine-6-phosphate deaminase]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Altamirano, M M.]]
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</StructureSection>
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[[Category: Calcagno, M L.]]
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[[Category: Escherichia coli K-12]]
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[[Category: Garratt, R C.]]
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[[Category: Large Structures]]
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[[Category: Horjales, E.]]
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[[Category: Altamirano MM]]
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[[Category: Oliva, G.]]
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[[Category: Calcagno ML]]
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[[Category: Aldose-ketose isomerase]]
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[[Category: Garratt RC]]
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[[Category: Allosteric enzyme]]
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[[Category: Horjales E]]
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[[Category: Entropic effect]]
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[[Category: Oliva G]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:36:01 2008''
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GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER

PDB ID 1cd5

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