NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE

S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE

Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms.

Crystallization of a Photosensitive Nitrile Hydratase from Rhodococcus Sp. N-771

SVTIDHTTENAAPAQAPVSDRAWALFRALDGKGLVPDGYVEGWKKTFEEDFSPRRGAELVARAWTDPEFRQLLLTDGTAA
VAQYGYLGPQGEYIVAVEDTPTLKNVIVCSL(CSD)S(CSO)TAWPILGLPPTWYKSFEYRARVVREPRKVLSEMGTEIA
SDIEIRVYDTTAETRYMVLPQRPAGTEGWSQEQLQEIVTKDCLIGVAIPQVPTV

SVTIDHTTENAAPAQAPVSDRAWALFRALDGKGLVPDGYVEGWKKTFEEDFSPRRGAELVARAWTDPEFRQLLLTDGTAA
VAQYGYLGPQGEYIVAVEDTPTLKNVIVCSLCSCTAWPILGLPPTWYKSFEYRARVVREPRKVLSEMGTEIASDIEIRVY
DTTAETRYMVLPQRPAGTEGWSQEQLQEIVTKDCLIGVAIPQVPTV

MDGVHDLAGVQGFGKVPHTVNADIGPTFHAEWEHLPYSLMFAGVAELGAFSVDEVRYVVERMEPRHYMMTPYYERYVIGV
ATLMVEKGILTQDELESLAGGPFPLSRPSESEGRPAPVETTTFEVGQRVRVRDEYVPGHIRMPAYCRGRVGTISHRTTEK
WPFPDAIGHGRNDAGEEPTYHVKFAAEELFGSDTDGGSVVVDLFEGYLEPAA

DATA WERE COLLECTED USING THE WEISSENBERG METHOD

THE NON-HEME IRON CENTER IS LOCATED AT THE INTERFACE
BETWEEN THE A AND B SUBUNIT.
THREE CYSTEINE RESIDUES, ONE SERINE RESIDUE IN THE
A SUBUNIT ARE COORDINATED TO THE NON-HEME IRON ATOM.
TWO OF THE THREE CYSTEINE RESIDUES (CYS 112 AND CYS 114)
ARE POST-TRANSLATIONALLY MODIFIED TO CYSTEINE SULFINIC
(112 CYS-SO2H) AND CYSTEINE SULFENIC (114 CYS-SOH) ACIDS.
THE SIXTH LIGAND IS AN ENDOGENOUS NO MOLECULE.

ALL ATOMS IN AN ASYMMETRIC UNIT WERE REFINED.

LYASE, PHOTOREACTIVE ENZYME, NITRIC OXIDE BINDING ENZYME, NON-HEME IRON CENTER, POST-TRANSLATIONAL MODIFICATION OF CYSTEINE RESIDUES, HYDRATASE

NON-HEME IRON CENTER AND CATALYTIC SITE IN CHAIN A

NON-HEME IRON CENTER AND CATALYTIC SITE IN CHAIN C