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| | ==Crystal structure of the unliganded (T-state) aspartate transcarbamoylase of the psychrophilic bacterium Moritella profunda== | | ==Crystal structure of the unliganded (T-state) aspartate transcarbamoylase of the psychrophilic bacterium Moritella profunda== |
| - | <StructureSection load='2be7' size='340' side='right' caption='[[2be7]], [[Resolution|resolution]] 2.85Å' scene=''> | + | <StructureSection load='2be7' size='340' side='right'caption='[[2be7]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2be7]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Jcm_11435 Jcm 11435]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BE7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2be7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Moritella_profunda Moritella profunda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=111291 JCM 11435]), pyrI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=111291 JCM 11435])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </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=2be7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2be7 OCA], [https://pdbe.org/2be7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2be7 RCSB], [https://www.ebi.ac.uk/pdbsum/2be7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2be7 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=2be7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2be7 OCA], [http://pdbe.org/2be7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2be7 RCSB], [http://www.ebi.ac.uk/pdbsum/2be7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2be7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYRI_VIBS2 PYRI_VIBS2]] Involved in allosteric regulation of aspartate carbamoyltransferase (By similarity). | + | [https://www.uniprot.org/uniprot/D0VWV8_MORPR D0VWV8_MORPR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2be7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2be7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspartate carbamoyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Jcm 11435]] | + | [[Category: Moritella profunda]] |
| - | [[Category: Beeumen, J Van]]
| + | [[Category: De Vos D]] |
| - | [[Category: Savvides, S N]]
| + | [[Category: Savvides SN]] |
| - | [[Category: Vos, D De]] | + | [[Category: Van Beeumen J]] |
| - | [[Category: Allosteric]] | + | |
| - | [[Category: Atcase]] | + | |
| - | [[Category: Cold adaptation]]
| + | |
| - | [[Category: Holoenzyme]]
| + | |
| - | [[Category: Psychrophilic]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
D0VWV8_MORPR
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
Aspartate carbamoyltransferase (EC 2.1.3.2) is extensively studied as a model for cooperativity and allosteric regulation. The structure of the Escherichia coli enzyme has been thoroughly analyzed by X-ray crystallography, and recently the crystal structures of two hyperthermophilic ATCases of the same structural class have been characterized. We here report the detailed functional and structural investigation of the ATCase from the psychrophilic deep sea bacterium Moritella profunda. Our analysis indicates that the enzyme conforms to the E. coli model in that two allosteric states exist that are influenced by similar homotropic interactions. The heterotropic properties differ in that CTP and UTP inhibit the holoenzyme, but ATP seems to exhibit a dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range. The crystal structure of the unliganded M. profunda ATCase shows resemblance to a more extreme T state reported previously for an E. coli ATCase mutant. A detailed molecular analysis reveals potential features of adaptation to cold activity and cold regulation. Moreover, M. profunda ATCase presents similarities with certain mutants of E. coli ATCase altered in their kinetic properties or temperature relationships. Finally, structural and functional comparison of ATCases across the full physiological temperature range agrees with an important, but fundamentally different role for electrostatics in protein adaptation at both extremes, i.e. an increased stability through the formation of ion pairs and ion pair networks at high physiological temperatures, and an increased flexibility through enhanced protein solvation at low temperatures.
Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda.,De Vos D, Xu Y, Hulpiau P, Vergauwen B, Van Beeumen JJ J Mol Biol. 2007 Jan 12;365(2):379-95. Epub 2006 Sep 29. PMID:17070547[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Vos D, Xu Y, Hulpiau P, Vergauwen B, Van Beeumen JJ. Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda. J Mol Biol. 2007 Jan 12;365(2):379-95. Epub 2006 Sep 29. PMID:17070547 doi:10.1016/j.jmb.2006.09.064
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