2CCW

Crystal structure of Azurin II at atomic resolution (1.13 angstrom)

Summary for 2CCW

• Entry DOI: 10.2210/pdb2ccw/pdb
• Related: 1DYZ 1DZ0
• Descriptor: AZURIN II, COPPER (I) ION (3 entities in total)
• Functional Keywords: electron transport (cuproprotein), azurin ii, alcaligenes xylosoxidans, electron transfer, cupredoxin, electron transport, cuproprotein, copper, metal- binding, periplasmic
• Biological source: ALCALIGENES XYLOSOXYDANS
• Cellular location: Periplasm: P56275
• Total number of polymer chains: 1
• Total formula weight: 13857.33

Authors

Paraskevopoulos, K.,Hough, M.A.,Eady, R.R.,Hasnain, S.S. (deposition date: 2006-01-18, release date: 2006-01-30, Last modification date: 2024-11-13)

Primary citation

Paraskevopoulos, K.,Sundararajan, M.,Surendran, R.,Hough, M.A.,Eady, R.R.,Hillier, I.H.,Hasnain, S.S.
Active Site Structures and the Redox Properties of Blue Copper Proteins: Atomic Resolution Structure of Azurin II and Electronic Structure Calculations of Azurin, Plastocyanin and Stellacyanin.
Dalton Trans., 25:3067-, 2006

PubMed Abstract: Understanding how the active site structures of blue copper proteins determine their redox properties is the central structure-function relationship question of this important class of protein, also referred to as cupredoxins. We here describe both experimental and computational studies of azurin, plastocyanin and stellacyanin designed to define more accurately the geometric structures of the active site of the reduced and oxidized species, and thus to understand how these structures determine the redox potentials of these proteins. To this end the crystal structure of reduced azurin II has been determined at an atomic resolution of 1.13 Angstrom and is presented here. Co-ordinates and structure factors have been deposited in the RCSB Protein Data Bank with accession codes 2ccw and r2ccwsf respectively. The improved accuracy provided by the atomic resolution for the metal stereochemistry are utilised in conjunction with the EXAFS data for theoretical calculations. Multilevel calculations involving density functional theory and molecular mechanical potentials are used to predict both the geometric and electronic structure of the active sites of azurin, plastocyanin and stellacyanin and to estimate the relative redox potentials of these three proteins. We have also compared the relative energies of the structures obtained from experiment at varying resolutions, and from the isolated and embedded cluster calculations. We find significant energy differences between low and high (atomic) resolution structures arising primarily due to inaccuracies in the Cu-ligand distances in the lower resolution structures, emphasising the importance of accurate, very high resolution structural information. QM/MM structures are only approximately 1 kcal mol(-1) lower in energy than the 1.13 Angstrom structure while the optimized gas phase structure is 13.0 kcal mol(-1) lower in energy.

PubMed: 16786065
DOI: 10.1039/B513942B

Experimental method

X-RAY DIFFRACTION (1.13 Å)