1F26: Crystal Structure Of No Complex Of Thr243val Mutants Of Cytochrome P450nor

Threonine 243 of cytochrome P450nor (fungal nitric oxide reductase) corresponds to the 'conserved' Thr in the long I helix of monooxygenase cytochrome P450s. In P450nor, the replacement of Thr243 with Asn, Ala or Val makes the enzymatic activity dramatically reduce. In order to understand the roles of Thr243 in the reduction reaction of NO by P450nor, the crystal structures of three Thr243 mutants (Thr243-->Asn, Thr243-->Val, Thr243-->Ala) of P450nor were determined at a 1.4-A resolution and at cryogenic temperature. However, the hydrogen-bonding pattern in the heme pocket of these mutants is essentially similar for that of the WT enzyme. This suggests that the determination of the structure of the NADH complex of P450nor is required, in order to evaluate the role of Thr243 in its enzymatic reaction. We attempted to crystallize the NADH complex under several conditions, but have not yet been successful.
PDB ID: 1F26Download
MMDB ID: 14507
PDB Deposition Date: 2000/5/23
Updated in MMDB: 2000/12
Experimental Method:
x-ray diffraction
Resolution: 1.4  Å
Source Organism:
Similar Structures:
Biological Unit for 1F26: monomeric; determined by author
Molecular Components in 1F26
Label Count Molecule
Protein (1 molecule)
Nitric Oxide Reductase
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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