2w43

From Proteopedia

(Difference between revisions)

Current revision

Structure of L-haloacid dehalogenase from S. tokodaii

Structural highlights

2w43 is a 2 chain structure with sequence from Sulfurisphaera tokodaii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.66Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q96XE7_SULTO

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

Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The L: -2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic L: -haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor L: -lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60 degrees C and a half-life of over 1 h at 70 degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO.

Biochemical and structural studies of a L: -haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii.,Rye CA, Isupov MN, Lebedev AA, Littlechild JA Extremophiles. 2008 Nov 29. PMID:19039518^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rye CA, Isupov MN, Lebedev AA, Littlechild JA. Biochemical and structural studies of a L: -haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii. Extremophiles. 2008 Nov 29. PMID:19039518 doi:10.1007/s00792-008-0208-0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w43"

@@ Line 3: / Line 3: @@
 <StructureSection load='2w43' size='340' side='right'caption='[[2w43]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2w43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_16993 Dsm 16993]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W43 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2w43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii Sulfurisphaera tokodaii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W43 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.66&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2w11|2w11]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Diisopropyl-fluorophosphatase Diisopropyl-fluorophosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.2 3.1.8.2] </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=2w43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w43 OCA], [https://pdbe.org/2w43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w43 RCSB], [https://www.ebi.ac.uk/pdbsum/2w43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w43 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q96XE7_SULTO Q96XE7_SULTO]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Diisopropyl-fluorophosphatase]]
-[[Category: Dsm 16993]]
 [[Category: Large Structures]]
-[[Category: Isupov, M N]]
+[[Category: Sulfurisphaera tokodaii]]
-[[Category: Lebedev, A A]]
+[[Category: Isupov MN]]
-[[Category: Littlechild, J A]]
+[[Category: Lebedev AA]]
-[[Category: Rye, C A]]
+[[Category: Littlechild JA]]
-[[Category: Hydrolase]]
+[[Category: Rye CA]]
-[[Category: Metabolic process]]

2w43

From Proteopedia

Current revision

Structure of L-haloacid dehalogenase from S. tokodaii

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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