1pwz: Difference between revisions
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<StructureSection load='1pwz' size='340' side='right'caption='[[1pwz]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1pwz' size='340' side='right'caption='[[1pwz]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pwz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1pwz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PWZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PWZ FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=RSO:R-STYRENE+OXIDE'>RSO</scene></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=1pwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwz OCA], [https://pdbe.org/1pwz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pwz RCSB], [https://www.ebi.ac.uk/pdbsum/1pwz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pwz 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=1pwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwz OCA], [https://pdbe.org/1pwz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pwz RCSB], [https://www.ebi.ac.uk/pdbsum/1pwz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pwz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q93D82_RHIRD Q93D82_RHIRD] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Agrobacterium tumefaciens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dijkstra | [[Category: Dijkstra BW]] | ||
[[Category: Janssen | [[Category: Janssen DB]] | ||
[[Category: Kalk KH]] | |||
[[Category: Kalk | [[Category: Rozeboom HJ]] | ||
[[Category: Rozeboom | [[Category: Tang L]] | ||
[[Category: Tang | [[Category: Tiesinga JJW]] | ||
[[Category: Tiesinga | [[Category: De Jong RM]] | ||
[[Category: | |||
Latest revision as of 12:49, 16 August 2023
Crystal structure of the haloalcohol dehalogenase HheC complexed with (R)-styrene oxide and chlorideCrystal structure of the haloalcohol dehalogenase HheC complexed with (R)-styrene oxide and chloride
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHaloalcohol dehalogenases are bacterial enzymes that catalyze the cofactor-independent dehalogenation of vicinal haloalcohols such as the genotoxic environmental pollutant 1,3-dichloro-2-propanol, thereby producing an epoxide, a chloride ion and a proton. Here we present X-ray structures of the haloalcohol dehalogenase HheC from Agrobacterium radiobacter AD1, and complexes of the enzyme with an epoxide product and chloride ion, and with a bound haloalcohol substrate mimic. These structures support a catalytic mechanism in which Tyr145 of a Ser-Tyr-Arg catalytic triad deprotonates the haloalcohol hydroxyl function to generate an intramolecular nucleophile that substitutes the vicinal halogen. Haloalcohol dehalogenases are related to the widespread family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDR family), which use a similar Ser-Tyr-Lys/Arg catalytic triad to catalyze reductive or oxidative conversions of various secondary alcohols and ketones. Our results reveal the first structural details of an SDR-related enzyme that catalyzes a substitutive dehalogenation reaction rather than a redox reaction, in which a halide-binding site is found at the location of the NAD(P)H binding site. Structure-based sequence analysis reveals that the various haloalcohol dehalogenases have likely originated from at least two different NAD-binding SDR precursors. Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site.,de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW EMBO J. 2003 Oct 1;22(19):4933-44. PMID:14517233[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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