5mxp

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==Haloalkane dehalogenase DmxA from Marinobacter sp. ELB17 possessing a unique catalytic residue==
==Haloalkane dehalogenase DmxA from Marinobacter sp. ELB17 possessing a unique catalytic residue==
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<StructureSection load='5mxp' size='340' side='right' caption='[[5mxp]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='5mxp' size='340' side='right'caption='[[5mxp]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mxp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MXP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mxp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinobacter_sp._ELB17 Marinobacter sp. ELB17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MXP FirstGlance]. <br>
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</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=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<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>
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<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=NA:SODIUM+ION'>NA</scene></td></tr>
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<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=5mxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mxp OCA], [http://pdbe.org/5mxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mxp RCSB], [http://www.ebi.ac.uk/pdbsum/5mxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mxp ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mxp OCA], [https://pdbe.org/5mxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mxp RCSB], [https://www.ebi.ac.uk/pdbsum/5mxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mxp ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A3JB27_9GAMM A3JB27_9GAMM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Haloalkane dehalogenases are enzymes with a broad application potential in biocatalysis, bioremediation, biosensing and cell imaging. The new haloalkane dehalogenase DmxA originating from the psychrophilic bacterium Marinobacter sp. ELB17 surprisingly possesses the highest thermal stability (apparent melting temperature Tm,app = 65.9 degrees C) of all biochemically characterized wild type haloalkane dehalogenases belonging to subfamily II. The enzyme was successfully expressed and its crystal structure was solved at 1.45 A resolution. DmxA structure contains several features distinct from known members of haloalkane dehalogenase family: (i) a unique composition of catalytic residues; (ii) a dimeric state mediated by a disulfide bridge; and (iii) narrow tunnels connecting the enzyme active site with the surrounding solvent. The importance of narrow tunnels in such paradoxically high stability of DmxA enzyme was confirmed by computational protein design and mutagenesis experiments.
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Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17.,Chrast L, Tratsiak K, Planas-Iglesias J, Daniel L, Prudnikova T, Brezovsky J, Bednar D, Kuta Smatanova I, Chaloupkova R, Damborsky J Microorganisms. 2019 Oct 28;7(11). pii: microorganisms7110498. doi:, 10.3390/microorganisms7110498. PMID:31661858<ref>PMID:31661858</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5mxp" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Haloalkane dehalogenase]]
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[[Category: Large Structures]]
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[[Category: Prudnikova, T]]
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[[Category: Marinobacter sp. ELB17]]
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[[Category: Rezacova, P]]
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[[Category: Prudnikova T]]
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[[Category: Tratsiak, K]]
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[[Category: Rezacova P]]
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[[Category: Disulfide bridge]]
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[[Category: Tratsiak K]]
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[[Category: Hydrolase]]
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[[Category: Thermostable enzyme]]
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[[Category: Unique catalytic residue]]
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Current revision

Haloalkane dehalogenase DmxA from Marinobacter sp. ELB17 possessing a unique catalytic residue

PDB ID 5mxp

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