2zcf

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|PDB= 2zcf |SIZE=350|CAPTION= <scene name='initialview01'>2zcf</scene>, resolution 1.43&Aring;
|PDB= 2zcf |SIZE=350|CAPTION= <scene name='initialview01'>2zcf</scene>, resolution 1.43&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= nthA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis]), nthB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis])
|GENE= nthA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis]), nthB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis])
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|DOMAIN=
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|RELATEDENTRY=[[1ahj|1AHJ]], [[2ahj|2AHJ]], [[2cyz|2CYZ]], [[2cz0|2CZ0]], [[2cz1|2CZ1]], [[2d0q|2D0Q]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcf OCA], [http://www.ebi.ac.uk/pdbsum/2zcf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zcf RCSB]</span>
}}
}}
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[[Category: Ueda, S.]]
[[Category: Ueda, S.]]
[[Category: Yohda, M.]]
[[Category: Yohda, M.]]
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[[Category: FE]]
 
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[[Category: MG]]
 
[[Category: cysteine-sulfenic acid]]
[[Category: cysteine-sulfenic acid]]
[[Category: cysteine-sulfinic acid]]
[[Category: cysteine-sulfinic acid]]
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:53:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:20:25 2008''

Revision as of 02:20, 31 March 2008

Image:2zcf.gif


PDB ID 2zcf

Drag the structure with the mouse to rotate
, resolution 1.43Å
Ligands: , , ,
Gene: nthA (Rhodococcus erythropolis), nthB (Rhodococcus erythropolis)
Activity: Nitrile hydratase, with EC number 4.2.1.84
Related: 1AHJ, 2AHJ, 2CYZ, 2CZ0, 2CZ1, 2D0Q


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771


Overview

Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic center, with glutamic acid or asparagine. The kcat of alphaQ90E and alphaQ90N mutants decreased to 24% and 5% that of wild type respectively, but the effect of mutations on Km was not very significant. In both mutants, the alphaCys114-SOH modification appeared to be responsible for the catalysis as in native NHase. We crystallized the nitrosylated alphaQ90N mutant and determined its structure at a resolution of 1.43 A. The structure was basically identical to that of native nitrosylated NHase except for the mutated site and its vicinity. The structural difference between native and alphaQ90N mutant NHases suggested the importance of the hydrogen bond networks between alphaGln90 and the iron center for the catalytic activity.

About this Structure

2ZCF is a Protein complex structure of sequences from Rhodococcus erythropolis. Full crystallographic information is available from OCA.

Reference

Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771., Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M, Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:16636455

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