2c9x

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[[Image:2c9x.gif|left|200px]]<br /><applet load="2c9x" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c9x.gif|left|200px]]
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caption="2c9x, resolution 1.80&Aring;" />
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'''SULFITE DEHYDROGENASE FROM STARKEYA NOVELLA Y236F MUTANT'''<br />
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{{Structure
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|PDB= 2c9x |SIZE=350|CAPTION= <scene name='initialview01'>2c9x</scene>, resolution 1.80&Aring;
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|SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MSS:(MOLYBDOPTERIN-S,S)-OXO-MOLYBDENUM'>MSS</scene> and <scene name='pdbligand=HEC:HEME C'>HEC</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''SULFITE DEHYDROGENASE FROM STARKEYA NOVELLA Y236F MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C9X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Starkeya_novella Starkeya novella] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MSS:'>MSS</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9X OCA].
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2C9X is a [[Protein complex]] structure of sequences 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].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16893171 16893171]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16893171 16893171]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Starkeya novella]]
[[Category: Starkeya novella]]
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[[Category: sulfite oxidase]]
[[Category: sulfite oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:46 2008''

Revision as of 14:12, 20 March 2008

Image:2c9x.gif


PDB ID 2c9x

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



SULFITE DEHYDROGENASE FROM STARKEYA NOVELLA Y236F MUTANT


Overview

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.

About this Structure

2C9X is a Protein complex structure of sequences from Starkeya novella. Full crystallographic information is available from OCA.

Reference

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

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