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| | <StructureSection load='4k2a' size='340' side='right'caption='[[4k2a]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4k2a' size='340' side='right'caption='[[4k2a]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k2a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49852 Atcc 49852]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K2A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_elkanii Bradyrhizobium elkanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K2A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </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></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a2m|3a2m]], [[2bn6|2bn6]], [[1cij|1cij]], [[2qvb|2qvb]], [[1cv2|1cv2]]</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=4k2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2a OCA], [https://pdbe.org/4k2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k2a RCSB], [https://www.ebi.ac.uk/pdbsum/4k2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k2a ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dbeA, dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29448 ATCC 49852])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2a OCA], [http://pdbe.org/4k2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k2a RCSB], [http://www.ebi.ac.uk/pdbsum/4k2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k2a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/E2RV62_BRAEL E2RV62_BRAEL]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons (By similarity).[HAMAP-Rule:MF_01231] | + | [https://www.uniprot.org/uniprot/E2RV62_BRAEL E2RV62_BRAEL] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons (By similarity).[HAMAP-Rule:MF_01231] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Dehalogenase|Dehalogenase]] | + | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 49852]] | + | [[Category: Bradyrhizobium elkanii]] |
| - | [[Category: Haloalkane dehalogenase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chaloupkova, R]] | + | [[Category: Chaloupkova R]] |
| - | [[Category: Damborsky, J]] | + | [[Category: Damborsky J]] |
| - | [[Category: Koudelakova, T]] | + | [[Category: Koudelakova T]] |
| - | [[Category: Kuty, M]] | + | [[Category: Kuta Smatanova I]] |
| - | [[Category: Mozga, T]] | + | [[Category: Kuty M]] |
| - | [[Category: Nagata, Y]] | + | [[Category: Mozga T]] |
| - | [[Category: Prudnikova, T]] | + | [[Category: Nagata Y]] |
| - | [[Category: Rezacova, P]] | + | [[Category: Prudnikova T]] |
| - | [[Category: S2F, Structure 2.Function Project]]
| + | [[Category: Rezacova P]] |
| - | [[Category: Sato, Y]] | + | [[Category: Sato Y]] |
| - | [[Category: Smatanova, I Kuta]]
| + | |
| - | [[Category: Dimer catalytic pentad]]
| + | |
| - | [[Category: Enzyme function initiative]]
| + | |
| - | [[Category: Halogen binding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: S2f]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structure 2 function project]]
| + | |
| - | [[Category: Two domain organization]]
| + | |
| Structural highlights
Function
E2RV62_BRAEL Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons (By similarity).[HAMAP-Rule:MF_01231]
Publication Abstract from PubMed
The crystal structure of the novel haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present in all structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift in the substrate-specificity class and were accompanied by a decrease in enzyme activity, stability and the elimination of substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step mediated by the lower basicity of the catalytic histidine.
Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites.,Chaloupkova R, Prudnikova T, Rezacova P, Prokop Z, Koudelakova T, Daniel L, Brezovsky J, Ikeda-Ohtsubo W, Sato Y, Kuty M, Nagata Y, Kuta Smatanova I, Damborsky J Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1884-97. doi:, 10.1107/S1399004714009018. Epub 2014 Jun 29. PMID:25004965[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chaloupkova R, Prudnikova T, Rezacova P, Prokop Z, Koudelakova T, Daniel L, Brezovsky J, Ikeda-Ohtsubo W, Sato Y, Kuty M, Nagata Y, Kuta Smatanova I, Damborsky J. Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites. Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1884-97. doi:, 10.1107/S1399004714009018. Epub 2014 Jun 29. PMID:25004965 doi:http://dx.doi.org/10.1107/S1399004714009018
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