|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1uwi' size='340' side='right'caption='[[1uwi]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='1uwi' size='340' side='right'caption='[[1uwi]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uwi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UWI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uwi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UWI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gow|1gow]]</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]] 2.55Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=1uwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwi OCA], [https://pdbe.org/1uwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uwi RCSB], [https://www.ebi.ac.uk/pdbsum/1uwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwi 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=1uwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwi OCA], [http://pdbe.org/1uwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uwi RCSB], [http://www.ebi.ac.uk/pdbsum/1uwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BGAL_SACS2 BGAL_SACS2] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 35: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-galactosidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulso]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Isorna, P]] | + | [[Category: Isorna P]] |
| - | [[Category: Polaina, J]] | + | [[Category: Polaina J]] |
| - | [[Category: Sanz-Aparicio, J]] | + | [[Category: Sanz-Aparicio J]] |
| - | [[Category: Beta-glycosidase]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
BGAL_SACS2
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
Comparison of the three-dimensional structure of hyperthermophilic and mesophilic beta-glycosidases shows differences in secondary structure composition. The enzymes from hyperthermophilic archaea have a significantly larger number of beta-strands arranged in supernumerary beta-sheets compared to mesophilic enzymes from bacteria and other organisms. Amino acid replacements designed to alter the structure of the supernumerary beta-strands were introduced by site directed mutagenesis into the sequence encoding the beta-glycosidase from Sulfolobus solfataricus. Most of the replacements caused almost complete loss of activity but some yielded enzyme variants whose activities were affected specifically at higher temperatures. Far-UV CD spectra recorded as a function of temperature for both wild type beta-glycosidase and mutant V349G, one of the mutants with reduced activity at higher temperatures, were similar, showing that the protein structure of the mutant was stable at the highest temperatures assayed. The properties of mutant V349G show a difference between thermostability (stability of the protein structure at high temperatures) and thermophilicity (optimal activity at high temperatures).
Comparative study and mutational analysis of distinctive structural elements of hyperthermophilic enzymes.,Leon M, Isorna P, Menendez M, Sanz-Aparicio J, Polaina J Protein J. 2007 Sep;26(6):435-44. PMID:17503162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leon M, Isorna P, Menendez M, Sanz-Aparicio J, Polaina J. Comparative study and mutational analysis of distinctive structural elements of hyperthermophilic enzymes. Protein J. 2007 Sep;26(6):435-44. PMID:17503162 doi:http://dx.doi.org/10.1007/s10930-007-9083-2
|
