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1fqo

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[[Image:1fqo.gif|left|200px]]
 
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==GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM)==
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The line below this paragraph, containing "STRUCTURE_1fqo", creates the "Structure Box" on the page.
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<StructureSection load='1fqo' size='340' side='right'caption='[[1fqo]], [[Resolution|resolution]] 2.20&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'>[[1fqo]] 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=1FQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQO 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]] 2.2&#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=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene></td></tr>
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{{STRUCTURE_1fqo| PDB=1fqo | SCENE= }}
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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=1fqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqo OCA], [https://pdbe.org/1fqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqo RCSB], [https://www.ebi.ac.uk/pdbsum/1fqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqo ProSAT]</span></td></tr>
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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/fq/1fqo_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=1fqo ConSurf].
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<div style="clear:both"></div>
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'''GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM)'''
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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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A new crystallographic structure of the free active-site R conformer of the allosteric enzyme glucosamine-6-phosphate deaminase from Escherichia coli, coupled with previously reported structures of the T and R conformers, generates a detailed description of the heterotropic allosteric transition in which structural flexibility plays a central role. The T conformer's external zone [Horjales et al. (1999), Structure, 7, 527-536] presents higher B values than in the R conformers. The ligand-free enzyme (T conformer) undergoes an allosteric transition to the free active-site R conformer upon binding of the allosteric activator. This structure shows three alternate conformations of the mobile section of the active-site lid (residues 163-182), in comparison to the high B values for the unique conformation of the T conformer. One of these alternate R conformations corresponds to the active-site lid found when the substrate is bound. The disorder associated with the three alternate conformations can be related to the biological regulation of the K(m) of the enzyme for the reaction, which is metabolically required to maintain adequate concentrations of the activator, which holds the enzyme in its R state. Seven alternate conformations for the active-site lid and three for the C-terminus were refined for the T structure using isotropic B factors. Some of these conformers approach that of the R conformer in geometry. Furthermore, the direction of the atomic vibrations obtained with anisotropic B refinement supports the hypothesis of an oscillating rather than a tense T state. The concerted character of the allosteric transition is also analysed in view of the apparent dynamics of the conformers.
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==About this Structure==
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1FQO 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=1FQO OCA].
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==Reference==
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Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase., Rudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):10-20. Epub 2001, Dec 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11752775 11752775]
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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: Horjales E]]
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[[Category: Horjales, E.]]
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[[Category: Morales-Arrieta S]]
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[[Category: Morales-Arrieta, S.]]
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[[Category: Rojas-Trejo SP]]
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[[Category: Rojas-Trejo, S P.]]
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[[Category: Rudino-Pinera E]]
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[[Category: Rudino-Pinera, E.]]
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[[Category: Aldose-ketose isomerase]]
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[[Category: Allosteric enzyme]]
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[[Category: Entropic effect]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:39:15 2008''
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Current revision

GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM)

PDB ID 1fqo

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