4wdq: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==Crystal structure of haloalkane dehalogenase LinB32 mutant (L177W) from Sphingobium japonicum UT26==

~~The entry~~ 4wdq is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4wdq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WDQ OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WDQ FirstGlance].

~~Authors~~: ~~Degtjarik~~, O., ~~Rezacova~~, P., ~~Chaloupkova~~, R., ~~Damborsky~~, J., ~~Kuta~~-~~Smatanova~~, I.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

~~Description~~: ~~Crystal structure of haloalkane~~ dehalogenase ~~LinB32 mutant (L177W) from Sphingobium japonicum UT26~~

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdq OCA], [http://pdbe.org/4wdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wdq RCSB], [http://www.ebi.ac.uk/pdbsum/4wdq PDBsum]</td></tr>

[[Category: ~~Unreleased Structures~~]]

</table>

== Function ==

[[http://www.uniprot.org/uniprot/LINB_SPHPI LINB_SPHPI]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols were good substrates. Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog. Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL).

__TOC__

</StructureSection>

[[Category: Haloalkane dehalogenase]]

[[Category: Chaloupkova, R]]

[[Category: Damborsky, J]]

[[Category: Degtjarik, O]]

[[Category: Kuta-Smatanova, I]]

~~[[Category: Damborsky, J]]~~

[[Category: Rezacova, P]]

[[Category: ~~Degtjarik, O~~]]

[[Category: Hydrolase]]

[[Category: ~~Chaloupkova, R~~]]

[[Category: Protein engineering]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of haloalkane dehalogenase LinB32 mutant (L177W) from Sphingobium japonicum UT26==
+<StructureSection load='4wdq' size='340' side='right' caption='[[4wdq]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
-The entry 4wdq is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wdq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WDQ FirstGlance]. <br>
-Authors: Degtjarik, O., Rezacova, P., Chaloupkova, R., Damborsky, J., Kuta-Smatanova, I.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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>
-Description: Crystal structure of haloalkane dehalogenase LinB32 mutant (L177W) from Sphingobium japonicum UT26
+<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=4wdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdq OCA], [http://pdbe.org/4wdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wdq RCSB], [http://www.ebi.ac.uk/pdbsum/4wdq PDBsum]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LINB_SPHPI LINB_SPHPI]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols were good substrates. Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog. Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL).
+__TOC__
+</StructureSection>
+[[Category: Haloalkane dehalogenase]]
+[[Category: Chaloupkova, R]]
+[[Category: Damborsky, J]]
+[[Category: Degtjarik, O]]
 [[Category: Kuta-Smatanova, I]]
-[[Category: Damborsky, J]]
 [[Category: Rezacova, P]]
-[[Category: Degtjarik, O]]
+[[Category: Hydrolase]]
-[[Category: Chaloupkova, R]]
+[[Category: Protein engineering]]