4HHG

Crystal structure of the Pseudomonas aeruginosa azurin, RuH107NO YOH109


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.235 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Electron Flow through Nitrotyrosinate in Pseudomonas aeruginosa Azurin.

Warren, J.J.Herrera, N.Hill, M.G.Winkler, J.R.Gray, H.B.

(2013) J Am Chem Soc 135: 11151-11158

  • DOI: https://doi.org/10.1021/ja403734n
  • Primary Citation of Related Structures:  
    4HHG, 4HHW, 4HIP

  • PubMed Abstract: 

    We have designed ruthenium-modified Pseudomonas aeruginosa azurins that incorporate 3-nitrotyrosine (NO2YOH) between Ru(2,2'-bipyridine)2(imidazole)(histidine) and Cu redox centers in electron transfer (ET) pathways. We investigated the structures and reactivities of three different systems: RuH107NO2YOH109, RuH124NO2YOH122, and RuH126NO2YOH122. RuH107NO2YOH109, unlabeled H124NO2YOH122, and unlabeled H126NO2YOH122 were structurally characterized. The pKa's of NO2YOH at positions 122 and 109 are 7.2 and 6.0, respectively. Reduction potentials of 3-nitrotyrosinate (NO2YO(-))-modified azurins were estimated from cyclic and differential pulse voltammetry data: oxidation of NO2YO(-)122 occurs near 1.1 versus NHE; oxidation of NO2YO(-)109 is near 1.2 V. Our analysis of transient optical spectroscopic experiments indicates that hopping via NO2YO(-) enhances Cu(I) oxidation rates over single-step ET by factors of 32 (RuH107NO2YO(-)109), 46 (RuH126NO2YO(-)122), and 13 (RuH124NO2YO(-)122).


  • Organizational Affiliation

    Beckman Institute and Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Azurin128Pseudomonas aeruginosa PAO1Mutation(s): 5 
Gene Names: azuPA4922
UniProt
Find proteins for P00282 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
Explore P00282 
Go to UniProtKB:  P00282
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00282
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DRU
Query on DRU

Download Ideal Coordinates CCD File 
C [auth A]DELTA-BIS(2,2'-BIPYRIDINE)IMIDAZOLE RUTHENIUM (II)
C23 H19 N6 Ru
ZSRBWSVKDUMHBO-UHFFFAOYSA-N
CU
Query on CU

Download Ideal Coordinates CCD File 
B [auth A]COPPER (II) ION
Cu
JPVYNHNXODAKFH-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
NIY
Query on NIY
A
L-PEPTIDE LINKINGC9 H10 N2 O5TYR
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.235 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.762α = 90
b = 67.176β = 90
c = 81.385γ = 90
Software Package:
Software NamePurpose
Blu-Icedata collection
MOLREPphasing
REFMACrefinement
autoXDSdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-11-21
    Type: Initial release
  • Version 1.1: 2013-07-31
    Changes: Database references
  • Version 1.2: 2013-08-21
    Changes: Database references