4h7h

From Proteopedia

(Difference between revisions)

Revision as of 08:03, 3 November 2022

Crystal structure of haloalkane dehalogenase LinB T135A mutant from Sphingobium sp. MI1205

Structural highlights

4h7h is a 1 chain structure with sequence from Sphingobium sp. MI1205. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A4PEU6_9SPHN Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons (By similarity).[HAMAP-Rule:MF_01231]

Publication Abstract from PubMed

The enzymes LinBUT and LinBMI (LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively) catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane (beta-HCH) and yield different products, 2,3,4,5,6-pentachlorocyclohexanol (PCHL) and 2,3,5,6-tetrachlorocyclohexane-1,4-diol (TCDL), respectively, despite their 98% identity in amino acid sequence. To reveal the structural basis of their different enzymatic properties, we performed site-directed mutagenesis and X-ray crystallographic studies of LinBMI and its seven point mutants. The mutation analysis revealed that the seven amino acid residues uniquely found in LinBMI were categorized into three groups based on the efficiency of the first-step (from beta-HCH to PCHL) and second-step (from PCHL to TCDL) conversions. Crystal structure analyses of wild-type LinBMI and its seven point mutants indicated how each mutated residue contributed to the first- and second-step conversions by LinBMI. The dynamics simulation analyses of wild-type LinBMI and LinBUT revealed that the entrance of the substrate access tunnel of LinBUT was more flexible than that of LinBMI, which could lead to the different efficiencies of dehalogenation activity between these dehalogenases.

Crystal Structure and Site-Directed Mutagenesis Analyses of Haloalkane Dehalogenase LinB from Sphingobium sp. Strain MI1205.,Okai M, Ohtsuka J, Imai LF, Mase T, Moriuchi R, Tsuda M, Nagata K, Nagata Y, Tanokura M J Bacteriol. 2013 Jun;195(11):2642-51. doi: 10.1128/JB.02020-12. Epub 2013 Apr 5. PMID:23564170^[1]

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

References

↑ Okai M, Ohtsuka J, Imai LF, Mase T, Moriuchi R, Tsuda M, Nagata K, Nagata Y, Tanokura M. Crystal Structure and Site-Directed Mutagenesis Analyses of Haloalkane Dehalogenase LinB from Sphingobium sp. Strain MI1205. J Bacteriol. 2013 Jun;195(11):2642-51. doi: 10.1128/JB.02020-12. Epub 2013 Apr 5. PMID:23564170 doi:10.1128/JB.02020-12

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4h7h"

@@ Line 1: / Line 1: @@
 ==Crystal structure of haloalkane dehalogenase LinB T135A mutant from Sphingobium sp. MI1205==
-<StructureSection load='4h7h' size='340' side='right' caption='[[4h7h]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='4h7h' size='340' side='right'caption='[[4h7h]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4h7h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphingobium_sp._mi1205 Sphingobium sp. mi1205]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H7H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4h7h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_sp._MI1205 Sphingobium sp. MI1205]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H7H FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4h77|4h77]], [[4h7d|4h7d]], [[4h7e|4h7e]], [[4h7f|4h7f]], [[4h7i|4h7i]], [[4h7j|4h7j]], [[4h7k|4h7k]]</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=4h7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h7h OCA], [https://pdbe.org/4h7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h7h RCSB], [https://www.ebi.ac.uk/pdbsum/4h7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h7h ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">linB, dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=407020 Sphingobium sp. MI1205])</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=4h7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h7h OCA], [http://pdbe.org/4h7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h7h RCSB], [http://www.ebi.ac.uk/pdbsum/4h7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h7h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A4PEU6_9SPHN A4PEU6_9SPHN]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons (By similarity).[HAMAP-Rule:MF_01231]
+[https://www.uniprot.org/uniprot/A4PEU6_9SPHN A4PEU6_9SPHN] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons (By similarity).[HAMAP-Rule:MF_01231]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 20: @@
 ==See Also==
-*[[Dehalogenase|Dehalogenase]]
+*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Sphingobium sp. mi1205]]
+[[Category: Large Structures]]
-[[Category: Imai, L F]]
+[[Category: Sphingobium sp. MI1205]]
-[[Category: Mase, T]]
+[[Category: Imai LF]]
-[[Category: Moriuchi, R]]
+[[Category: Mase T]]
-[[Category: Nagata, K]]
+[[Category: Moriuchi R]]
-[[Category: Nagata, Y]]
+[[Category: Nagata K]]
-[[Category: Ohtsuka, J]]
+[[Category: Nagata Y]]
-[[Category: Okai, M]]
+[[Category: Ohtsuka J]]
-[[Category: Tanokura, M]]
+[[Category: Okai M]]
-[[Category: Tsuda, M]]
+[[Category: Tanokura M]]
-[[Category: Alpha/beta hydrolase fold]]
+[[Category: Tsuda M]]
-[[Category: Hydrolase]]

4h7h

From Proteopedia

Revision as of 08:03, 3 November 2022

Crystal structure of haloalkane dehalogenase LinB T135A mutant from Sphingobium sp. MI1205

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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