PDBsum entry 1akd

Oxidoreductase

PDB id: 1akd

Contents

Protein chain

405 a.a. *

Ligands

HEM

CAM

Metals

__K

Waters ×271

* Residue conservation analysis

PDB id:

1akd

Name:

Oxidoreductase

Title:

Cytochrome p450cam from pseudomonas putida, complexed with 1s-camphor

Structure:

Cytochrome p450cam. Chain: a. Synonym: camphor monooxygenase. Engineered: yes. Other_details: heme linked by cys 357, substrate (1s)-camphor bound in two conformations, a and b

Source:

Pseudomonas putida. Organism_taxid: 303. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.80Å R-factor: 0.209 R-free: 0.265

Authors:

I.Schlichting,C.Jung,H.Schulze

Key ref:

I.Schlichting et al. (1997). Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer. Febs Lett, 415, 253-257. PubMed id: 9357977 DOI: 10.1016/S0014-5793(97)01135-6

Date:

16-May-97 Release date: 19-Nov-97

Protein chain

P00183  (CPXA_PSEPU) -  Camphor 5-monooxygenase from Pseudomonas putida

Seq: 415 a.a.

Struc: 405 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.1.14.15.1 - camphor 5-monooxygenase.
• Reaction: 2 reduced [2Fe-2S]-[putidaredoxin] + (1R,4R)-camphor + O2 + 2 H⁺ = (1R,4R,5R)-5-hydroxycamphor + 2 oxidized [2Fe-2S]-[putidaredoxin] + H2O
• Cofactor: Heme-thiolate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

DOI no: 10.1016/S0014-5793(97)01135-6

Febs Lett 415:253-257 (1997)

PubMed id: 9357977

Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.

I.Schlichting, C.Jung, H.Schulze.

ABSTRACT

The crystal structure of cytochrome P-450cam complexed with the enantiomer (1S)-camphor has been solved to 1.8 angstroms resolution and compared with the structure of the (1R)-camphor P-450cam complex. The overall protein structure is the same for both enantiomer complexes. However, the orientation of the substrates in the heme pocket differs. In contrast to (1R)-camphor, the (1S)-enantiomer binds in at least two orientations. The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quinone group of camphor, and the 10-methyl group points towards the I-helix. The binding differs in that C-5 is not at a position suitable for hydroxylation. In the other orientation (1S)-camphor is not hydrogen bonded, but C-5 is located suitably for hydroxylation.

Selected figure(s)

Figure 1.
Fig. 1. Stereoview of the two orientations of (1S)-camphor in a (3F[obs]-2F[calc]) electron density map. The electron density is shown at a σ-level of 1.0. The higher occupied orientation (corresponding to ‘first orientation' in Table 2 and Table 3) is shown in a. The lower occupied orientation (corresponding to ‘second orientation' in Table 2 and Table 3) is shown in b. The orientation of the camphor molecules is the same as in Fig. 2. The figure was generated using MOLSCRIPT [14].

Figure 2.
Fig. 2. View of the two (1S)-camphor conformations (b, c) in the heme pocket in comparison to the (1R)-camphor orientation (a). The higher occupied orientation of (1S)-camphor (corresponding to ‘first orientation' in Table 2 and Table 3) is shown in b. Camphor is shown in relation to the heme, part of the I-helix and Tyr-96. The figure was generated using MOLSCRIPT [14].

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Febs Lett (1997, 415, 253-257) copyright 1997.