1g4h

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{{Seed}}
 
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[[Image:1g4h.png|left|200px]]
 
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==LINB COMPLEXED WITH BUTAN-1-OL==
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The line below this paragraph, containing "STRUCTURE_1g4h", creates the "Structure Box" on the page.
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<StructureSection load='1g4h' size='340' side='right'caption='[[1g4h]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1g4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_paucimobilis Sphingomonas paucimobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G4H FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1BO:1-BUTANOL'>1BO</scene>, <scene name='pdbligand=2MR:N3,+N4-DIMETHYLARGININE'>2MR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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{{STRUCTURE_1g4h| PDB=1g4h | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4h OCA], [https://pdbe.org/1g4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g4h RCSB], [https://www.ebi.ac.uk/pdbsum/1g4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g4h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LINB_SPHIU LINB_SPHIU] 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 since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols are good substrates (PubMed:10100638, PubMed:9293022). Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog (PubMed:9293022). Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL) (PubMed:7691794). This degradation pathway allows S.japonicum UT26 to grow on gamma-HCH as the sole source of carbon and energy.<ref>PMID:10100638</ref> <ref>PMID:7691794</ref> <ref>PMID:9293022</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g4/1g4h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1g4h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The hydrolysis of haloalkanes to their corresponding alcohols and inorganic halides is catalyzed by alpha/beta-hydrolases called haloalkane dehalogenases. The study of haloalkane dehalogenases is vital for the development of these enzymes if they are to be utilized for bioremediation of organohalide-contaminated industrial waste. We report the kinetic and structural analysis of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) in complex with each of 1,2-dichloroethane and 1,2-dichloropropane and the reaction product of 1-chlorobutane turnover. Activity studies showed very weak but detectable activity of LinB with 1,2-dichloroethane [0.012 nmol s(-1) (mg of enzyme)(-1)] and 1,2-dichloropropane [0.027 nmol s(-1) (mg of enzyme)(-1)]. These activities are much weaker compared, for example, to the activity of LinB with 1-chlorobutane [68.2 nmol s(-1) (mg of enzyme)(-1)]. Inhibition analysis reveals that both 1,2-dichloroethane and 1,2-dichloropropane act as simple competitive inhibitors of the substrate 1-chlorobutane and that 1,2-dichloroethane binds to LinB with lower affinity than 1,2-dichloropropane. Docking calculations on the enzyme in the absence of active site water molecules and halide ions confirm that these compounds could bind productively. However, when these moieties were included in the calculations, they bound in a manner similar to that observed in the crystal structure. These data provide an explanation for the low activity of LinB with small, chlorinated alkanes and show the importance of active site water molecules and reaction products in molecular docking.
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===LINB COMPLEXED WITH BUTAN-1-OL===
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Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition.,Oakley AJ, Prokop Z, Bohac M, Kmunicek J, Jedlicka T, Monincova M, Kuta-Smatanova I, Nagata Y, Damborsky J, Wilce MC Biochemistry. 2002 Apr 16;41(15):4847-55. PMID:11939779<ref>PMID:11939779</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1g4h" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11939779}}, adds the Publication Abstract to the page
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*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11939779 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11939779}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1G4H is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_paucimobilis Sphingomonas paucimobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4H OCA].
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==Reference==
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<ref group="xtra">PMID:11939779</ref><references group="xtra"/>
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[[Category: Sphingomonas paucimobilis]]
[[Category: Sphingomonas paucimobilis]]
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[[Category: Bohac, M.]]
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[[Category: Bohac M]]
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[[Category: Damborsky, J.]]
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[[Category: Damborsky J]]
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[[Category: Jedlicka, T.]]
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[[Category: Jedlicka T]]
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[[Category: Kmunicek, J.]]
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[[Category: Kmunicek J]]
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[[Category: Kuta-Smatanova, I.]]
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[[Category: Kuta-Smatanova I]]
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[[Category: Monincova, M.]]
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[[Category: Monincova M]]
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[[Category: Nagata, Y.]]
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[[Category: Nagata Y]]
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[[Category: Oakley, A J.]]
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[[Category: Oakley AJ]]
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[[Category: Prokop, Z.]]
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[[Category: Prokop Z]]
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[[Category: Wilce, M C.J.]]
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[[Category: Wilce MCJ]]
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[[Category: Linb haloalkane dehalogenase halocarbon]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:12:18 2009''
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Current revision

LINB COMPLEXED WITH BUTAN-1-OL

PDB ID 1g4h

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