1psd

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(New page: 200px<br /><applet load="1psd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psd, resolution 2.75&Aring;" /> '''THE ALLOSTERIC LIGAN...)
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[[Image:1psd.gif|left|200px]]<br /><applet load="1psd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1psd, resolution 2.75&Aring;" />
 
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'''THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE'''<br />
 
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==Overview==
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==THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE==
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The crystal structure of the phosphoglycerate dehydrogenase from, Escherichia coli is unique among dehydrogenases. It consists of three, clearly separate domains connected by flexible hinges. The tetramer has, approximate 222 symmetry with the principal contacts between the subunits, forming between either the nucleotide binding domains or the regulatory, domains. Two slightly different subunit conformations are present which, vary only in the orientations of the domains. There is a hinge-like, arrangement near the active site cleft and the serine effector site is, provided by the regulatory domain of each of two subunits. Interdomain, flexibility may play a key role in both catalysis and allosteric, inhibition.
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<StructureSection load='1psd' size='340' side='right'caption='[[1psd]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1psd]] is a 2 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=1PSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PSD FirstGlance]. <br>
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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]] 2.75&#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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></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=1psd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psd OCA], [https://pdbe.org/1psd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1psd RCSB], [https://www.ebi.ac.uk/pdbsum/1psd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1psd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SERA_ECOLI SERA_ECOLI]
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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/ps/1psd_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=1psd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1PSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12] with NAD and SER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_dehydrogenase Phosphoglycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.95 1.1.1.95] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSD OCA].
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*[[Phosphoglycerate dehydrogenase|Phosphoglycerate dehydrogenase]]
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__TOC__
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==Reference==
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</StructureSection>
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The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase., Schuller DJ, Grant GA, Banaszak LJ, Nat Struct Biol. 1995 Jan;2(1):69-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7719856 7719856]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli k12]]
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[[Category: Large Structures]]
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[[Category: Phosphoglycerate dehydrogenase]]
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[[Category: Banaszak LJ]]
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[[Category: Single protein]]
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[[Category: Grant GA]]
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[[Category: Banaszak, L.J.]]
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[[Category: Schuller DJ]]
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[[Category: Grant, G.A.]]
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[[Category: Schuller, D.J.]]
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[[Category: NAD]]
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[[Category: SER]]
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[[Category: oxidoreductase (nad(a))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:05:04 2007''
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Current revision

THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE

PDB ID 1psd

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