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1oih

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Revision as of 23:44, 10 September 2015

CRYSTAL STRUCTURE OF THE ALKYLSULFATASE ATSK, A NON-HEME FE(II) ALPHAKETOGLUTARATE DEPENDENT DIOXYGENASE

Structural highlights

1oih is a 4 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1oii, 1oij, 1oik
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ATSK_PSEPU] Catalyzes the oxigenolytic cleavage of 2-ethylhexyl sulfate (2-EHS) in the presence of alpha-ketoglutarate to yield 2-ethyl-hexanal and succinate, the decarboxylated form of alpha-ketoglutarate. It can accepte a wide range of alpha-keto acids including 2-oxo-valerate, 2-oxo-adipate, 2-oxo-octanoate, 3-methyl-2-oxo-butyrate, oxaloacetate-alpha-ketoadipate, and alpha-ketooctanoate. It can catalyze the cleavage of medium-chain alkyl sulfate esters such as butylsulfate, pentylsulfate, hexylsulfate, heptylsulfate, octylsulfate, nonylsulfate, decylsulfate and sodium dodecyl sulfate (SDS).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The alkylsulfatase AtsK from Pseudomonas putida S-313 belongs to the widespread and versatile non-heme iron(II) alpha-ketoglutarate-dependent dioxygenase superfamily and catalyzes the oxygenolytic cleavage of a variety of different alkyl sulfate esters to the corresponding aldehyde and sulfate. The enzyme is only expressed under sulfur starvation conditions, providing a selective advantage for bacterial growth in soils and rhizosphere. Here we describe the crystal structure of AtsK in the apo form and in three complexes: with the cosubstrate alpha-ketoglutarate, with alpha-ketoglutarate and iron, and finally with alpha-ketoglutarate, iron, and an alkyl sulfate ester used as substrate in catalytic studies. The overall fold of the enzyme is closely related to that of the taurine/alpha-ketoglutarate dioxygenase TauD and is similar to the fold observed for other members of the enzyme superfamily. From comparison of these structures with the crystal structure of AtsK and its complexes, we propose a general mechanism for the catalytic cycle of the alpha-ketoglutarate-dependent dioxygenase superfamily.

Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily.,Muller I, Kahnert A, Pape T, Sheldrick GM, Meyer-Klaucke W, Dierks T, Kertesz M, Uson I Biochemistry. 2004 Mar 23;43(11):3075-88. PMID:15023059^[2]

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

References

↑ Kahnert A, Kertesz MA. Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313. J Biol Chem. 2000 Oct 13;275(41):31661-7. PMID:10913158 doi:http://dx.doi.org/10.1074/jbc.M005820200
↑ Muller I, Kahnert A, Pape T, Sheldrick GM, Meyer-Klaucke W, Dierks T, Kertesz M, Uson I. Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily. Biochemistry. 2004 Mar 23;43(11):3075-88. PMID:15023059 doi:http://dx.doi.org/10.1021/bi035752v

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oih"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oii|1oii]], [[1oij|1oij]], [[1oik|1oik]]</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=1oih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oih RCSB], [http://www.ebi.ac.uk/pdbsum/1oih PDBsum]</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=1oih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oih OCA], [http://pdbe.org/1oih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oih RCSB], [http://www.ebi.ac.uk/pdbsum/1oih PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ATSK_PSEPU ATSK_PSEPU]] Catalyzes the oxigenolytic cleavage of 2-ethylhexyl sulfate (2-EHS) in the presence of alpha-ketoglutarate to yield 2-ethyl-hexanal and succinate, the decarboxylated form of alpha-ketoglutarate. It can accepte a wide range of alpha-keto acids including 2-oxo-valerate, 2-oxo-adipate, 2-oxo-octanoate, 3-methyl-2-oxo-butyrate, oxaloacetate-alpha-ketoadipate, and alpha-ketooctanoate. It can catalyze the cleavage of medium-chain alkyl sulfate esters such as butylsulfate, pentylsulfate, hexylsulfate, heptylsulfate, octylsulfate, nonylsulfate, decylsulfate and sodium dodecyl sulfate (SDS).<ref>PMID:10913158</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1oih" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1oih

From Proteopedia

Revision as of 23:44, 10 September 2015

CRYSTAL STRUCTURE OF THE ALKYLSULFATASE ATSK, A NON-HEME FE(II) ALPHAKETOGLUTARATE DEPENDENT DIOXYGENASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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