This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3rk4

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:34, 5 August 2016

Structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant DhaA31

Structural highlights

3rk4 is a 1 chain structure with sequence from "bacterium_mycoides_roseum"_grotenfelt_1889 "bacterium mycoides roseum" grotenfelt 1889. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3fbw, 3g9x, 3fwh, 1bn6, 1cqw, 3rlt
Gene:	dhaA, DhaA31 ("Bacterium mycoides roseum" Grotenfelt 1889)
Activity:	Haloalkane dehalogenase, with EC number 3.8.1.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DHAA_RHORH] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.

Publication Abstract from PubMed

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds, which is a key step in the aerobic mineralization of many environmental pollutants. One important pollutant is the toxic and anthropogenic compound 1,2,3-trichloropropane (TCP). Rational design was combined with saturation mutagenesis to obtain the haloalkane dehalogenase variant DhaA31, which displays an increased catalytic activity towards TCP. Here, the 1.31 A resolution crystal structure of substrate-free DhaA31, the 1.26 A resolution structure of DhaA31 in complex with TCP and the 1.95 A resolution structure of wild-type DhaA are reported. Crystals of the enzyme-substrate complex were successfully obtained by adding volatile TCP to the reservoir after crystallization at pH 6.5 and room temperature. Comparison of the substrate-free structure with that of the DhaA31 enzyme-substrate complex reveals that the nucleophilic Asp106 changes its conformation from an inactive to an active state during the catalytic cycle. The positions of three chloride ions found inside the active site of the enzyme indicate a possible pathway for halide release from the active site through the main tunnel. Comparison of the DhaA31 variant with wild-type DhaA revealed that the introduced substitutions reduce the volume and the solvent-accessibility of the active-site pocket.

Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31.,Lahoda M, Mesters JR, Stsiapanava A, Chaloupkova R, Kuty M, Damborsky J, Kuta Smatanova I Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):209-17. doi:, 10.1107/S1399004713026254. Epub 2014 Jan 17. PMID:24531456^[1]

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

References

↑ Lahoda M, Mesters JR, Stsiapanava A, Chaloupkova R, Kuty M, Damborsky J, Kuta Smatanova I. Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):209-17. doi:, 10.1107/S1399004713026254. Epub 2014 Jan 17. PMID:24531456 doi:http://dx.doi.org/10.1107/S1399004713026254

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3rk4"

@@ Line 1: / Line 1: @@
 ==Structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant DhaA31==
 <StructureSection load='3rk4' size='340' side='right' caption='[[3rk4]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaA, DhaA31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1829 "Bacterium mycoides roseum" Grotenfelt 1889])</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=3rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rk4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rk4 RCSB], [http://www.ebi.ac.uk/pdbsum/3rk4 PDBsum]</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=3rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rk4 OCA], [http://pdbe.org/3rk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rk4 RCSB], [http://www.ebi.ac.uk/pdbsum/3rk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rk4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3rk4" style="background-color:#fffaf0;"></div>
 ==See Also==

3rk4

From Proteopedia

Revision as of 13:34, 5 August 2016

Structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant DhaA31

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox