5JQU: Crystal Structure Of Cytochrome P450 Bm3 Heme Domain G265f/t269v/l272w/l322i/f405m/a406s (wivs-fm) Variant With Iron(iii) Deuteroporphyrin Ix Bound

Citation:
Abstract
We introduce a strategy that expands the functionality of hemoproteins through orthogonal enzyme/heme pairs. By exploiting the ability of a natural heme transport protein, ChuA, to promiscuously import heme derivatives, we have evolved a cytochrome P450 (P450BM3) that selectively incorporates a nonproteinogenic cofactor, iron deuteroporphyrin IX (Fe-DPIX), even in the presence of endogenous heme. Crystal structures show that selectivity gains are due to mutations that introduce steric clash with the heme vinyl groups while providing a complementary binding surface for the smaller Fe-DPIX cofactor. Furthermore, the evolved orthogonal enzyme/cofactor pair is active in non-natural carbenoid-mediated olefin cyclopropanation. This methodology for the generation of orthogonal enzyme/cofactor pairs promises to expand cofactor diversity in artificial metalloenzymes.
PDB ID: 5JQUDownload
MMDB ID: 143551
PDB Deposition Date: 2016/5/5
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.16  Å
Source Organism:
Similar Structures:
Biological Unit for 5JQU: octameric; determined by author and by software (PISA)
Molecular Components in 5JQU
Label Count Molecule
Proteins (8 molecules)
8
Bifunctional Cytochrome P450/nadph--p450 Reductase
Molecule annotation
Chemicals (8 molecules)
1
8
* Click molecule labels to explore molecular sequence information.

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