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2c9x

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Revision as of 21:39, 9 September 2015

SULFITE DEHYDROGENASE FROM STARKEYA NOVELLA Y236F MUTANT

Structural highlights

2c9x is a 2 chain structure with sequence from Atcc 8093. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2blf, 2bpb, 2ca3, 2ca4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[Q9LA16_STANO] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.[SAAS:SAAS00086612] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase (By similarity).

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 sulfite dehydrogenase from Starkeya novella is the only known sulfite-oxidizing enzyme that forms a permanent heterodimeric complex between a molybdenum and a heme c-containing subunit and can be crystallized in an electron transfer competent conformation. Tyr236 is a highly conserved active site residue in sulfite oxidoreductases and has been shown to interact with a nearby arginine and a molybdenum-oxo ligand that is involved in catalysis. We have created a Tyr236 to Phe substitution in the SorAB sulfite dehydrogenase. The purified SDH(Y236F) protein has been characterized in terms of activity, structure, intramolecular electron transfer, and EPR properties. The substituted protein exhibited reduced turnover rates and substrate affinity as well as an altered reactivity toward molecular oxygen as an electron acceptor. Following reduction by sulfite and unlike SDH(WT), the substituted enzyme was reoxidized quickly in the presence of molecular oxygen, a process reminiscent of the reactions of the sulfite oxidases. SDH(Y236F) also exhibited the pH-dependent CW-EPR signals that are typically observed in vertebrate sulfite oxidases, allowing a direct link of CW-EPR properties to changes caused by a single-amino acid substitution. No quantifiable electron transfer was seen in laser flash photolysis experiments with SDH(Y236F). The crystal structure of SDH(Y236F) clearly shows that as a result of the substitution the hydrogen bonding network surrounding the active site is disturbed, resulting in an increased mobility of the nearby arginine. These disruptions underline the importance of Tyr236 for the integrity of the substrate binding site and the optimal alignment of Arg55, which appears to be necessary for efficient electron transfer.

Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase.,Kappler U, Bailey S, Feng C, Honeychurch MJ, Hanson GR, Bernhardt PV, Tollin G, Enemark JH Biochemistry. 2006 Aug 15;45(32):9696-705. PMID:16893171^[1]

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

References

↑ Kappler U, Bailey S, Feng C, Honeychurch MJ, Hanson GR, Bernhardt PV, Tollin G, Enemark JH. Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase. Biochemistry. 2006 Aug 15;45(32):9696-705. PMID:16893171 doi:10.1021/bi060058b

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/2c9x"

@@ Line 2: / Line 2: @@
 <StructureSection load='2c9x' size='340' side='right' caption='[[2c9x]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c9x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Starkeya_novella Starkeya novella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c9x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_8093 Atcc 8093]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9X FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MSS:(MOLYBDOPTERIN-S,S)-OXO-MOLYBDENUM'>MSS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2blf|2blf]], [[2bpb|2bpb]], [[2ca3|2ca3]], [[2ca4|2ca4]]</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=2c9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c9x RCSB], [http://www.ebi.ac.uk/pdbsum/2c9x 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=2c9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9x OCA], [http://pdbe.org/2c9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c9x RCSB], [http://www.ebi.ac.uk/pdbsum/2c9x PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q9LA16_STANO Q9LA16_STANO]] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.[SAAS:SAAS00086612]  The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase (By similarity).
 == 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 2c9x" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Starkeya novella]]
+[[Category: Atcc 8093]]
 [[Category: Bailey, S]]
 [[Category: Bernhardt, P]]

2c9x

From Proteopedia

Revision as of 21:39, 9 September 2015

SULFITE DEHYDROGENASE FROM STARKEYA NOVELLA Y236F MUTANT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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