|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1bvu' size='340' side='right'caption='[[1bvu]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1bvu' size='340' side='right'caption='[[1bvu]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bvu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BVU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bvu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVU FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></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]] 2.5Å</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=1bvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvu OCA], [http://pdbe.org/1bvu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bvu RCSB], [http://www.ebi.ac.uk/pdbsum/1bvu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvu 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=1bvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvu OCA], [https://pdbe.org/1bvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bvu RCSB], [https://www.ebi.ac.uk/pdbsum/1bvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DHE3_THELN DHE3_THELN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 37: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Thermococcus litoralis]] | | [[Category: Thermococcus litoralis]] |
| - | [[Category: Baker, P J]] | + | [[Category: Baker PJ]] |
| - | [[Category: Britton, K L]] | + | [[Category: Britton KL]] |
| - | [[Category: Rice, D W]] | + | [[Category: Rice DW]] |
| - | [[Category: Stillman, T J]] | + | [[Category: Stillman TJ]] |
| - | [[Category: Yip, K S]] | + | [[Category: Yip KS]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Thermal stability]]
| + | |
| Structural highlights
Function
DHE3_THELN
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
Glutamate dehydrogenase catalyses the oxidative deamination of glutamate to 2-oxoglutarate with concomitant reduction of NAD(P)(+), and has been shown to be widely distributed in nature across species ranging from psychrophiles to hyperthermophiles. Extensive characterisation of this enzyme isolated from hyperthermophilic organisms has led to its adoption as a model system for analysing the determinants of thermal stability. The crystal structure of the extremely thermostable glutamate dehydrogenase from Thermococcus litoralis has been determined at 2.5 A resolution, and has been compared to that from the hyperthermophile Pyrococcus furiosus. The two enzymes are 87 % identical in sequence, yet differ 16-fold in their half-lives at 104 degrees C. This is the first reported comparative analysis of the structures of a multisubunit enzyme from two closely related yet distinct hyperthermophilies. The less stable T. litoralis enzyme has a decreased number of ion pair interactions; modified patterns of hydrogen bonding resulting from isosteric sequence changes; substitutions that decrease packing efficiency; and substitutions which give rise to subtle but distinct shifts in both main-chain and side-chain elements of the structure. This analysis provides a rational basis to test ideas on the factors that confer thermal stability in proteins through a combination of mutagenesis, calorimetry, and structural studies.
Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus.,Britton KL, Yip KS, Sedelnikova SE, Stillman TJ, Adams MW, Ma K, Maeder DL, Robb FT, Tolliday N, Vetriani C, Rice DW, Baker PJ J Mol Biol. 1999 Nov 12;293(5):1121-32. PMID:10547290[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Britton KL, Yip KS, Sedelnikova SE, Stillman TJ, Adams MW, Ma K, Maeder DL, Robb FT, Tolliday N, Vetriani C, Rice DW, Baker PJ. Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus. J Mol Biol. 1999 Nov 12;293(5):1121-32. PMID:10547290 doi:10.1006/jmbi.1999.3205
|
