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2ahj

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[[Image:2ahj.gif|left|200px]]<br /><applet load="2ahj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ahj.gif|left|200px]]<br /><applet load="2ahj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ahj, resolution 1.7&Aring;" />
caption="2ahj, resolution 1.7&Aring;" />
'''NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE'''<br />
'''NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE'''<br />
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==About this Structure==
==About this Structure==
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2AHJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis] with FE, ZN, SO4, NO and DIO as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Sites: <scene name='pdbsite=1:In Chain C'>1</scene>, <scene name='pdbsite=CTA:Non-Heme Fe Center And Catalytic Site Site_description I ...'>CTA</scene> and <scene name='pdbsite=CTB:In Chain A Site_identifier Ctb Site_description Non-Heme ...'>CTB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AHJ OCA].
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2AHJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NO:'>NO</scene> and <scene name='pdbligand=DIO:'>DIO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Sites: <scene name='pdbsite=1:In+Chain+C'>1</scene>, <scene name='pdbsite=CTA:Non-Heme+Fe+Center+And+Catalytic+Site+Site_description+I+...'>CTA</scene> and <scene name='pdbsite=CTB:In+Chain+A+Site_identifier+Ctb+Site_description+Non-Heme+...'>CTB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHJ OCA].
==Reference==
==Reference==
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[[Category: post-translational modification of cysteine residues]]
[[Category: post-translational modification of cysteine residues]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:43:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:22:55 2008''

Revision as of 08:22, 3 February 2008


2ahj, resolution 1.7Å

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NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE

Overview

The iron-containing nitrile hydratase (NHase) is a photoreactive enzyme, that is inactivated in the dark because of persistent association with NO, and activated by photo-dissociation of NO. The crystal structure at 1.7 A, resolution and mass spectrometry revealed the structure of the non-heme, iron catalytic center in the nitrosylated state. Two Cys residues, coordinated to the iron were post-translationally modified to Cys-sulfenic, and -sulfinic acids. Together with another oxygen atom of the Ser ligand, these modifications induced a claw setting of oxygen atoms capturing an NO, molecule. This unprecedented structure is likely to enable the, photo-regulation of NHase and will provide an excellent model for, designing photo-controllable chelate complexes and, ultimately, proteins.

About this Structure

2AHJ is a Protein complex structure of sequences from Rhodococcus erythropolis with , , , and as ligands. Active as Nitrile hydratase, with EC number 4.2.1.84 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

Reference

Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms., Nagashima S, Nakasako M, Dohmae N, Tsujimura M, Takio K, Odaka M, Yohda M, Kamiya N, Endo I, Nat Struct Biol. 1998 May;5(5):347-51. PMID:9586994

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