1VLX

STRUCTURE OF ELECTRON TRANSFER (COBALT-PROTEIN)

1VLX の概要

• エントリーDOI: 10.2210/pdb1vlx/pdb
• 分子名称: AZURIN, COBALT (II) ION (3 entities in total)
• 機能のキーワード: electron transport, copper, periplasmic
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Periplasm: P00282
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56082.93

構造登録者

Bonander, N.,Vanngard, T.,Tsai, L.-C.,Langer, V.,Nar, H.,Sjolin, L. (登録日: 1996-10-08, 公開日: 1997-03-12, 最終更新日: 2024-10-16)

主引用文献

Bonander, N.,Vanngard, T.,Tsai, L.C.,Langer, V.,Nar, H.,Sjolin, L.
The metal site of Pseudomonas aeruginosa azurin, revealed by a crystal structure determination of the Co(II) derivative and Co-EPR spectroscopy.
Proteins, 27:385-394, 1997

PubMed Abstract: The crystal structure of cobalt-substituted azurin from Pseudomonas aeruginosa has been determined to final crystallographic R value of 0.175 at 1.9 A resolution. There are four molecules in the asymmetric unit in the structure, and these four molecules are packed as a dimer of dimers. The dimer packing is very similar to that of the wild-type Pseudomonas aeruginosa azurin dimer. Replacement of the native copper by the cobalt ion has only small effects on the metal binding site presumably because of the existence of an extensive network of hydrogen bonds in its immediate neighborhood. Some differences are obvious, however. In wild-type azurin the copper atom occupies a distorted trigonal bipyramidal site, while cobalt similar to zinc and nickel occupy a distorted tetrahedral site, in which the distance to the Met121,S(delta) atom is increased to 3.3-3.5 A and the distance to the carbonyl oxygen of Gly45 has decreased to 2.1-2.4 A. The X-band EPR spectrum of the high-spin Co(II) in azurin is well resolved (apparent g values gx' = 5.23; gy' = 3.83; gz' = 1.995, and hyperfine splittings Ax' = 31; Ay' = 20-30; Az' = 53 G) and indicates that the ligand field is close to axial.

PubMed: 9094740
DOI: 10.1002/(SICI)1097-0134(199703)27:3<385::AID-PROT6>3.0.CO;2-C

実験手法

X-RAY DIFFRACTION (1.9 Å)