4brz
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4brz is ON HOLD until Paper Publication Authors: Novak, H.R., Sayer, C., Isupov, M., Gotz, D., Spragg, A.M., Littlechild, J.A. Description: Haloalk...) |
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- | '''Unreleased structure''' | ||
- | + | ==Haloalkane dehalogenase== | |
+ | <StructureSection load='4brz' size='340' side='right'caption='[[4brz]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4brz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacteraceae Rhodobacteraceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BRZ FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4brz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brz OCA], [https://pdbe.org/4brz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4brz RCSB], [https://www.ebi.ac.uk/pdbsum/4brz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4brz ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A067XG63_9RHOB A0A067XG63_9RHOB] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A deeper substrate binding pocket defines the enzyme preference towards substrates with longer carbon chains. Arg136 at the bottom of the substrate pocket is positioned to bind the distal halogen group of extended di-halogenated substrates. | ||
- | + | Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae.,Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA FEBS Lett. 2014 May 2;588(9):1616-22. doi: 10.1016/j.febslet.2014.02.056. Epub, 2014 Mar 5. PMID:24613925<ref>PMID:24613925</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 4brz" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Rhodobacteraceae]] | ||
+ | [[Category: Gotz D]] | ||
+ | [[Category: Isupov M]] | ||
+ | [[Category: Littlechild JA]] | ||
+ | [[Category: Novak HR]] | ||
+ | [[Category: Sayer C]] | ||
+ | [[Category: Spragg AM]] |
Current revision
Haloalkane dehalogenase
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