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| | <StructureSection load='2v0y' size='340' side='right'caption='[[2v0y]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2v0y' size='340' side='right'caption='[[2v0y]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v0y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v0y]] is a 1 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=2V0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c44|2c44]], [[2v1p|2v1p]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1] </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=2v0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0y OCA], [https://pdbe.org/2v0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0y RCSB], [https://www.ebi.ac.uk/pdbsum/2v0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0y 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=2v0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0y OCA], [https://pdbe.org/2v0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0y RCSB], [https://www.ebi.ac.uk/pdbsum/2v0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TNAA_ECOLI TNAA_ECOLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tryptophanase]]
| + | [[Category: Almog O]] |
| - | [[Category: Almog, O]] | + | [[Category: Cohen-Luria R]] |
| - | [[Category: Cohen-Luria, R]] | + | [[Category: Gdalevsky GY]] |
| - | [[Category: Gdalevsky, G Y]] | + | [[Category: Goldgur Y]] |
| - | [[Category: Goldgur, Y]] | + | [[Category: Kogan A]] |
| - | [[Category: Kogan, A]] | + | [[Category: Parola AH]] |
| - | [[Category: Parola, A H]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Tryptophan catabolism]]
| + | |
| Structural highlights
Function
TNAA_ECOLI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
BACKGROUND: Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP is covalently bound through an enamine bond to Lys270 at the active site. The incubation of holo E. coli Trpases at 2 degrees C for 20 h results in breaking this enamine bond and PLP release, as well as a reversible loss of activity and dissociation into dimers. This sequence of events is termed cold lability and its understanding bears relevance to protein stability and shelf life. RESULTS: We studied the reversible cold lability of E. coli Trpase and its Y74F, C298S and W330F mutants. In contrast to the holo E. coli Trpase all apo forms of Trpase dissociated into dimers already at 25 degrees C and even further upon cooling to 2 degrees C. The crystal structures of the two mutants, Y74F and C298S in their apo form were determined at 1.9A resolution. These apo mutants were found in an open conformation compared to the closed conformation found for P. vulgaris in its holo form. This conformational change is further supported by a high pressure study. CONCLUSION: We suggest that cold lability of E. coli Trpases is primarily affected by PLP release. The enhanced loss of activity of the three mutants is presumably due to the reduced size of the side chain of the amino acids. This prevents the tight assembly of the active tetramer, making it more susceptible to the cold driven changes in hydrophobic interactions which facilitate PLP release. The hydrophobic interactions along the non catalytic interface overshadow the effect of point mutations and may account for the differences in the dissociation of E. coli Trpase to dimers and P. vulgaris Trpase to monomers.
Conformational changes and loose packing promote E. coli Tryptophanase cold lability.,Kogan A, Gdalevsky GY, Cohen-Luria R, Goldgur Y, Phillips RS, Parola AH, Almog O BMC Struct Biol. 2009 Oct 8;9:65. PMID:19814824[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kogan A, Gdalevsky GY, Cohen-Luria R, Goldgur Y, Phillips RS, Parola AH, Almog O. Conformational changes and loose packing promote E. coli Tryptophanase cold lability. BMC Struct Biol. 2009 Oct 8;9:65. PMID:19814824 doi:10.1186/1472-6807-9-65
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