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==CRYSTAL STRUCTURE OF haloalkane dehalogenase (DccA) from Caulobacter crescentus== | |||
<StructureSection load='5esr' size='340' side='right' caption='[[5esr]], [[Resolution|resolution]] 1.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5esr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESR FirstGlance]. <br> | |||
</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=CO:COBALT+(II)+ION'>CO</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> | |||
<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=5esr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5esr OCA], [http://pdbe.org/5esr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5esr RCSB], [http://www.ebi.ac.uk/pdbsum/5esr PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/DHMA_CAUCR DHMA_CAUCR]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two putative haloalkane dehalogenases (HLDs) of the HLD-I subfamily, DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea, have been identified based on sequence comparisons with functionally characterized HLD enzymes. The two genes were synthesized, functionally expressed in E. coli and shown to have activity toward a panel of haloalkane substrates. DsaA has a moderate activity level and a preference for long (greater than 3 carbons) brominated substrates, but little activity toward chlorinated alkanes. DccA shows high activity with both long brominated and chlorinated alkanes. The structure of DccA was determined by X-ray crystallography and was refined to 1.5 A resolution. The enzyme has a large and open binding pocket with two well-defined access tunnels. A structural alignment of HLD-I subfamily members suggests a possible basis for substrate specificity is due to access tunnel size. | |||
Biochemical characterization of two haloalkane dehalogenases: DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea.,Carlucci L, Zhou E, Malashkevich VN, Almo SC, Mundorff EC Protein Sci. 2016 Apr;25(4):877-86. doi: 10.1002/pro.2895. Epub 2016 Feb 21. PMID:26833751<ref>PMID:26833751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5esr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Haloalkane dehalogenase]] | |||
[[Category: ALMO, S C]] | |||
[[Category: MALASHKEVICH, V N]] | |||
[[Category: Mundorff, E C]] | |||
[[Category: Toro, R]] | [[Category: Toro, R]] | ||
[[Category: | [[Category: Hydrolase]] | ||
Revision as of 18:32, 1 June 2016
CRYSTAL STRUCTURE OF haloalkane dehalogenase (DccA) from Caulobacter crescentusCRYSTAL STRUCTURE OF haloalkane dehalogenase (DccA) from Caulobacter crescentus
Structural highlights
Function[DHMA_CAUCR] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Publication Abstract from PubMedTwo putative haloalkane dehalogenases (HLDs) of the HLD-I subfamily, DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea, have been identified based on sequence comparisons with functionally characterized HLD enzymes. The two genes were synthesized, functionally expressed in E. coli and shown to have activity toward a panel of haloalkane substrates. DsaA has a moderate activity level and a preference for long (greater than 3 carbons) brominated substrates, but little activity toward chlorinated alkanes. DccA shows high activity with both long brominated and chlorinated alkanes. The structure of DccA was determined by X-ray crystallography and was refined to 1.5 A resolution. The enzyme has a large and open binding pocket with two well-defined access tunnels. A structural alignment of HLD-I subfamily members suggests a possible basis for substrate specificity is due to access tunnel size. Biochemical characterization of two haloalkane dehalogenases: DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea.,Carlucci L, Zhou E, Malashkevich VN, Almo SC, Mundorff EC Protein Sci. 2016 Apr;25(4):877-86. doi: 10.1002/pro.2895. Epub 2016 Feb 21. PMID:26833751[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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