5ZLH

Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.346 
  • R-Value Work: 0.310 
  • R-Value Observed: 0.312 

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Literature

Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A.

Omura, K., Aiba, Y., Onoda, H., Stanfield, J.K., Ariyasu, S., Sugimoto, H., Shiro, Y., Shoji, O., Watanabe, Y.

(2018) Chem Commun (Camb) 54: 7892-7895

  • DOI: https://doi.org/10.1039/c8cc02760a
  • Primary Citation of Related Structures:  
    5ZIS, 5ZLH

  • PubMed Abstract: 

    Haem substitution is an effective approach to tweak the function of haemoproteins. Herein, we report a facile haem substitution method for self-sufficient cytochrome P450BM3 (CYP102A1) from Bacillus megaterium utilising the transpeptidase Sortase A from Staphylococcus aureus. We successfully constructed Mn-substituted BM3 and investigated its catalytic activity.

    • Organizational Affiliation: 

    Department of Chemistry, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-0802, Japan. [email protected].


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bifunctional cytochrome P450/NADPH--P450 reductase
A, B, C, D
455Priestia megateriumMutation(s): 0 
Gene Names: BTA37_15100
EC: 1.14.14.1 (PDB Primary Data), 1.6.2.4 (PDB Primary Data)
UniProt
Find proteins for P14779 (Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19))
Explore P14779 
Go to UniProtKB:  P14779
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP14779
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.346 
  • R-Value Work: 0.310 
  • R-Value Observed: 0.312 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.76α = 90
b = 155.32β = 90
c = 208.98γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
PDB_EXTRACTdata extraction

Structure Validation

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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Japan Science and TechnologyJapanJPMJCR15P3
Ministry of Education, Culture, Sports, Science and Technology (Japan)Japan17H03087

Revision History  (Full details and data files)

  • Version 1.0: 2018-08-15
    Type: Initial release
  • Version 1.1: 2024-03-27
    Changes: Data collection, Database references