1psd
From Proteopedia
(Difference between revisions)
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<StructureSection load='1psd' size='340' side='right'caption='[[1psd]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='1psd' size='340' side='right'caption='[[1psd]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1psd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id=' | + | <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> |
<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> | <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> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SERA_ECOLI SERA_ECOLI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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:7719856<ref>PMID:7719856</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1psd" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Phosphoglycerate dehydrogenase|Phosphoglycerate dehydrogenase]] | *[[Phosphoglycerate dehydrogenase|Phosphoglycerate dehydrogenase]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Banaszak LJ]] | |
| - | [[Category: Banaszak | + | [[Category: Grant GA]] |
| - | [[Category: Grant | + | [[Category: Schuller DJ]] |
| - | [[Category: Schuller | + | |
Current revision
THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE
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