Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip.
作者： Herbert Nar , Albrecht Messerschmidt , Robert Huber , Mart van de Kamp , Gerard W. Canters
DOI: 10.1016/0022-2836(91)80173-R
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摘要: The X-ray crystal structure of recombinant wild-type azurin from Pseudomonas aeruginosa was determined by difference Fourier techniques using phases derived the mutant His35Leu. Two data sets were collected a single oxidized soaked in mother liquor buffered at pH 5.5 and 9.0, respectively. Both extend to 1.93 A resolution. two forms refined independently crystallographic R-factors 17.6% (pH 5.5) 17.5% 9.0). conformational transition previously attributed protonation/deprotonation residue His35 (pKa(red) = 7.3, pKa(ox) 6.2), which lies crevice protein close copper binding site, involves concomitant Pro36-Gly37 main-chain peptide bond flip. At lower pH, protonated imidazole N delta 1 strong hydrogen with carbonyl oxygen Pro36, while alkaline deprotonated acts as an acceptor weak HN Gly37. remainder molecule, including is not significantly affected this transition.
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elsevier.com参考文章(38)
Crystallography in molecular biology Plenum Press. ,(1987) , 10.1007/978-1-4684-5272-3
Gerard W. CANTERS, H. Allen O. HILL, Nicholas A. KITCHEN, Elinor T. ADMAN, The assignment of the 1H nuclear magnetic resonance spectrum of azurin. An investigation of the 1H NMR spectrum of the blue copper protein, azurin, from Pseudomonas aeruginosa, with reference to the previously determined crystal structure. FEBS Journal. ,vol. 138, pp. 141- 152 ,(1984) , 10.1111/J.1432-1033.1984.TB07893.X
G.W. Canters, The azurin gene from Pseudomonas aeruginosa
codes for a pre-protein with a signal peptide FEBS Letters. ,vol. 212, pp. 168- 172 ,(1987) , 10.1016/0014-5793(87)81579-X
C M Groeneveld, G W Canters, NMR study of structure and electron transfer mechanism of Pseudomonas aeruginosa azurin. Journal of Biological Chemistry. ,vol. 263, pp. 167- 173 ,(1988) , 10.1016/S0021-9258(19)57374-4
Eraldo Antonini, Alessandro Finazzi-Agrò, Luciana Avigliano, Pietro Guerrieri, G. Rotilio, Bruno Mondovì, Kinetics of Electron Transfer between Azurin and Cytochrome 551 from Pseudomonas Journal of Biological Chemistry. ,vol. 245, pp. 4847- 4849 ,(1970) , 10.1016/S0021-9258(18)62870-4
T. A. Jones, A graphics model building and refinement system for macromolecules Journal of Applied Crystallography. ,vol. 11, pp. 268- 272 ,(1978) , 10.1107/S0021889878013308
Ole Farver, Israel Pecht, Affinity Labeling of an Electron Transfer Pathway in Azurin by Cr(II) Ions Israel Journal of Chemistry. ,vol. 21, pp. 13- 17 ,(1981) , 10.1002/IJCH.198100004
Edward N. Baker, Structure of azurin from Alcaligenes denitrificans refinement at 1.8 A resolution and comparison of the two crystallographically independent molecules. Journal of Molecular Biology. ,vol. 203, pp. 1071- 1095 ,(1987) , 10.1016/0022-2836(88)90129-5
C.M. Groeneveld, M.C. Ouwerling, C. Erkelens, G.W. Canters, 1H nuclear magnetic resonance study of the protonation behaviour of the histidine residues and the electron self-exchange reaction of azurin from Alcaligenes denitrificans. Journal of Molecular Biology. ,vol. 200, pp. 189- 199 ,(1988) , 10.1016/0022-2836(88)90343-9
LARS RYDEN, JAN-OLOF LUNDGREN, Homology relationships among the small blue proteins. Nature. ,vol. 261, pp. 344- 346 ,(1976) , 10.1038/261344A0