1ire: Difference between revisions
New page: left|200px<br /><applet load="1ire" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ire, resolution 1.80Å" /> '''Crystal Structure of... |
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[[Image:1ire.gif|left|200px]]<br /><applet load="1ire" size=" | [[Image:1ire.gif|left|200px]]<br /><applet load="1ire" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ire, resolution 1.80Å" /> | caption="1ire, resolution 1.80Å" /> | ||
'''Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila'''<br /> | '''Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of cobalt-containing nitrile hydratase from | The crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two cysteine residues (alphaCys(111) and alphaCys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (betaTrp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase. | ||
==About this Structure== | ==About this Structure== | ||
1IRE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudonocardia_thermophila Pseudonocardia thermophila] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] Full crystallographic information is available from [http:// | 1IRE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudonocardia_thermophila Pseudonocardia thermophila] with <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: post-translational modification]] | [[Category: post-translational modification]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:47 2008'' | ||
Revision as of 14:14, 21 February 2008
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Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
OverviewOverview
The crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two cysteine residues (alphaCys(111) and alphaCys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (betaTrp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase.
About this StructureAbout this Structure
1IRE is a Protein complex structure of sequences from Pseudonocardia thermophila with as ligand. Active as Nitrile hydratase, with EC number 4.2.1.84 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cobalt-containing nitrile hydratase., Miyanaga A, Fushinobu S, Ito K, Wakagi T, Biochem Biophys Res Commun. 2001 Nov 16;288(5):1169-74. PMID:11700034
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