2dhe

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Revision as of 07:06, 29 November 2017

CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE

Structural highlights

2dhe is a 1 chain structure with sequence from "corynebacterium_autotrophicum"_baumgarten_et_al._1974 "corynebacterium autotrophicum" baumgarten et al. 1974. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Haloalkane dehalogenase, with EC number 3.8.1.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DHLA_XANAU] 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, which includes terminally mono- and di- chlorinated and brominated alkanes (up to C4 only). The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane.

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

Crystal structures of haloalkane dehalogenase were determined in the presence of the substrate 1,2-dichloroethane. At pH 5 and 4 degrees C, substrate is bound in the active site without being converted; warming to room temperature causes the substrate's carbon-chlorine bond to be broken, producing a chloride ion with concomitant alkylation of the active-site residue Asp124. At pH 6 and room temperature the alkylated enzyme is hydrolysed by a water molecule activated by the His289-Asp260 pair in the active site. These results show that catalysis by the dehalogenase proceeds by a two-step mechanism involving an ester intermediate covalently bound at Asp124.

Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase.,Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW Nature. 1993 Jun 24;363(6431):693-8. PMID:8515812^[1]

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

References

↑ Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature. 1993 Jun 24;363(6431):693-8. PMID:8515812 doi:http://dx.doi.org/10.1038/363693a0

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Corynebacterium autotrophicum baumgarten et al. 1974 | Haloalkane dehalogenase | Dijkstra, B W | Verschueren, K H.G | Dehalogenase

@@ Line 1: / Line 1: @@
 ==CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE==
 <StructureSection load='2dhe' size='340' side='right' caption='[[2dhe]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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>
-<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=2dhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhe OCA], [http://pdbe.org/2dhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dhe RCSB], [http://www.ebi.ac.uk/pdbsum/2dhe 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=2dhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhe OCA], [http://pdbe.org/2dhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dhe RCSB], [http://www.ebi.ac.uk/pdbsum/2dhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhe ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dhe ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2dhe" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Dehalogenase|Dehalogenase]]
 == References ==
 <references/>

2dhe

From Proteopedia

Revision as of 07:06, 29 November 2017

CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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