6f9o: Difference between revisions

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-'''Unreleased structure'''
-The entry 6f9o is ON HOLD
+==Crystal structure of cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5==
+<StructureSection load='6f9o' size='340' side='right'caption='[[6f9o]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6f9o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Psyck Psyck]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F9O 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhmA, Pcryo_1253 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=335284 PSYCK])</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=6f9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f9o OCA], [http://pdbe.org/6f9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f9o RCSB], [http://www.ebi.ac.uk/pdbsum/6f9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f9o ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DHMA_PSYCK DHMA_PSYCK]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.[HAMAP-Rule:MF_01230]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Haloalkane dehalogenases (HLDs) convert halogenated aliphatic pollutants to less toxic compounds by a hydrolytic mechanism. Owing to their broad substrate specificity and high enantioselectivity, haloalkane dehalogenases can function as biosensors to detect toxic compounds in the environment or can be used for the production of optically pure compounds. Here, the structural analysis of the haloalkane dehalogenase DpcA isolated from the psychrophilic bacterium Psychrobacter cryohalolentis K5 is presented at the atomic resolution of 1.05 A. This enzyme exhibits a low temperature optimum, making it attractive for environmental applications such as biosensing at the subsurface environment, where the temperature typically does not exceed 25 degrees C. The structure revealed that DpcA possesses the shortest access tunnel and one of the most widely open main tunnels among structural homologs of the HLD-I subfamily. Comparative analysis revealed major differences in the region of the alpha4 helix of the cap domain, which is one of the key determinants of the anatomy of the tunnels. The crystal structure of DpcA will contribute to better understanding of the structure-function relationships of cold-adapted enzymes.
-Authors:
+Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5.,Tratsiak K, Prudnikova T, Drienovska I, Damborsky J, Brynda J, Pachl P, Kuty M, Chaloupkova R, Rezacova P, Kuta Smatanova I Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):324-331. doi:, 10.1107/S2053230X19002796. Epub 2019 Apr 24. PMID:31045561<ref>PMID:31045561</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6f9o" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Haloalkane dehalogenase]]
+[[Category: Large Structures]]
+[[Category: Psyck]]
+[[Category: Brynda, J]]
+[[Category: Chaloupkova, R]]
+[[Category: Damborsky, J]]
+[[Category: Drienovska, I]]
+[[Category: Kuty, M]]
+[[Category: Pachl, P]]
+[[Category: Prudnikova, T]]
+[[Category: Rezacova, P]]
+[[Category: Smatanova, I Kuta]]
+[[Category: Tratsiak, K]]
+[[Category: 1-bromohexane and 1]]
+[[Category: Domain]]
+[[Category: 3-dibromopropane]]
+[[Category: Alpha/beta-hydrolase fold enzyme]]
+[[Category: Hld]]
+[[Category: Hydrolase]]
+[[Category: Microbial enzyme]]
+[[Category: The highest activity towards 1-bromobutane]]