|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3g9x' size='340' side='right'caption='[[3g9x]], [[Resolution|resolution]] 0.95Å' scene=''> | | <StructureSection load='3g9x' size='340' side='right'caption='[[3g9x]], [[Resolution|resolution]] 0.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhoso Rhoso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_sp. Rhodococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 0.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fbw|3fbw]], [[3fwh|3fwh]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1831 RHOSO])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </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=3g9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9x OCA], [https://pdbe.org/3g9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9x RCSB], [https://www.ebi.ac.uk/pdbsum/3g9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9x 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=3g9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9x OCA], [https://pdbe.org/3g9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9x RCSB], [https://www.ebi.ac.uk/pdbsum/3g9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DHAA_RHOSO DHAA_RHOSO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 36: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haloalkane dehalogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rhoso]] | + | [[Category: Rhodococcus sp]] |
| - | [[Category: Dohnalek, J]] | + | [[Category: Dohnalek J]] |
| - | [[Category: Gavira, J A]] | + | [[Category: Gavira JA]] |
| - | [[Category: Kuty, M]] | + | [[Category: Kuta Smatanova I]] |
| - | [[Category: Lapkouski, M]] | + | [[Category: Kuty M]] |
| - | [[Category: Smatanova, I Kuta]] | + | [[Category: Lapkouski M]] |
| - | [[Category: Stsiapanava, A]] | + | [[Category: Stsiapanava A]] |
| - | [[Category: Alpha/beta hydrolase]]
| + | |
| - | [[Category: Detoxification]]
| + | |
| - | [[Category: Haloalkane]]
| + | |
| - | [[Category: Helical cap domain]]
| + | |
| - | [[Category: His272]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: I135f]]
| + | |
| - | [[Category: Mutant]]
| + | |
| Structural highlights
Function
DHAA_RHOSO
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
The haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 is a bacterial enzyme that shows catalytic activity for the hydrolytic degradation of the highly toxic industrial pollutant 1,2,3-trichloropropane (TCP). Mutagenesis focused on the access tunnels of DhaA produced protein variants with significantly improved activity towards TCP. Three mutants of DhaA named DhaA04 (C176Y), DhaA14 (I135F) and DhaA15 (C176Y + I135F) were constructed in order to study the functional relevance of the tunnels connecting the buried active site of the protein with the surrounding solvent. All three protein variants were crystallized using the sitting-drop vapour-diffusion technique. The crystals of DhaA04 belonged to the orthorhombic space group P2(1)2(1)2(1), while the crystals of DhaA14 and DhaA15 had triclinic symmetry in space group P1. The crystal structures of DhaA04, DhaA14 and DhaA15 with ligands present in the active site were solved and refined using diffraction data to 1.23, 0.95 and 1.22 A, resolution, respectively. Structural comparisons of the wild type and the three mutants suggest that the tunnels play a key role in the processes of ligand exchange between the buried active site and the surrounding solvent.
Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels.,Stsiapanava A, Dohnalek J, Gavira JA, Kuty M, Koudelakova T, Damborsky J, Kuta Smatanova I Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):962-9. Epub 2010, Aug 13. PMID:20823547[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stsiapanava A, Dohnalek J, Gavira JA, Kuty M, Koudelakova T, Damborsky J, Kuta Smatanova I. Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):962-9. Epub 2010, Aug 13. PMID:20823547 doi:10.1107/S0907444910027101
|
