|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='5c2x' size='340' side='right'caption='[[5c2x]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='5c2x' size='340' side='right'caption='[[5c2x]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_psychroerythrus"_d'aoust_and_kushner_1972 "vibrio psychroerythrus" d'aoust and kushner 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C2X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Colwellia_psychrerythraea Colwellia psychrerythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C2X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 2.11Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">deoC, CPS_1972 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28229 "Vibrio psychroerythrus" D'Aoust and Kushner 1972])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase Deoxyribose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.4 4.1.2.4] </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=5c2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c2x OCA], [https://pdbe.org/5c2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c2x RCSB], [https://www.ebi.ac.uk/pdbsum/5c2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c2x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c2x OCA], [http://pdbe.org/5c2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c2x RCSB], [http://www.ebi.ac.uk/pdbsum/5c2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c2x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q483R4_COLP3 Q483R4_COLP3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio psychroerythrus d'aoust and kushner 1972]] | + | [[Category: Colwellia psychrerythraea]] |
| - | [[Category: Deoxyribose-phosphate aldolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dick, M]] | + | [[Category: Dick M]] |
| - | [[Category: Pietruszka, J]] | + | [[Category: Pietruszka J]] |
| - | [[Category: Weiergraeber, O H]] | + | [[Category: Weiergraeber OH]] |
| - | [[Category: Dera]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Psychrophilic]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
Q483R4_COLP3
Publication Abstract from PubMed
Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs from psychrophilic, mesophilic and hyperthermophilic organisms. We present the first crystal structures of psychrophilic DERAs, revealing a dimeric organization resembling their mesophilic but not their thermophilic counterparts. Conversion into monomeric proteins showed that the native dimer interface contributes to stability only in the hyperthermophilic enzymes. Nevertheless, introduction of a disulfide bridge in the interface of a psychrophilic DERA did confer increased thermostability, suggesting a strategy for rational design of more durable enzyme variants. Constraint network analysis revealed particularly sparse interactions between the substrate pocket and its surrounding alpha-helices in psychrophilic DERAs, which indicates that a more flexible active center underlies their high turnover numbers.
Trading off stability against activity in extremophilic aldolases.,Dick M, Weiergraber OH, Classen T, Bisterfeld C, Bramski J, Gohlke H, Pietruszka J Sci Rep. 2016 Jan 19;6:17908. doi: 10.1038/srep17908. PMID:26783049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dick M, Weiergraber OH, Classen T, Bisterfeld C, Bramski J, Gohlke H, Pietruszka J. Trading off stability against activity in extremophilic aldolases. Sci Rep. 2016 Jan 19;6:17908. doi: 10.1038/srep17908. PMID:26783049 doi:http://dx.doi.org/10.1038/srep17908
|
