1v29: Difference between revisions
New page: left|200px<br /><applet load="1v29" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v29, resolution 2.6Å" /> '''Crystal structure of ... |
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[[Image:1v29.gif|left|200px]]<br /><applet load="1v29" size=" | [[Image:1v29.gif|left|200px]]<br /><applet load="1v29" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1v29, resolution 2.6Å" /> | caption="1v29, resolution 2.6Å" /> | ||
'''Crystal structure of Nitrile hydratase from a thermophile Bacillus smithii'''<br /> | '''Crystal structure of Nitrile hydratase from a thermophile Bacillus smithii'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the nitrile hydratase (NHase) from Bacillus | The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme. | ||
==About this Structure== | ==About this Structure== | ||
1V29 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_smithii Bacillus smithii] 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:// | 1V29 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_smithii Bacillus smithii] 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=1V29 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nhase]] | [[Category: nhase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:50 2008'' | ||
Revision as of 16:30, 21 February 2008
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Crystal structure of Nitrile hydratase from a thermophile Bacillus smithii
OverviewOverview
The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme.
About this StructureAbout this Structure
1V29 is a Protein complex structure of sequences from Bacillus smithii 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 nitrile hydratase from a thermophilic Bacillus smithii., Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K, Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142
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