2APS

CU/ZN SUPEROXIDE DISMUTASE FROM ACTINOBACILLUS PLEUROPNEUMONIAE

2APS の概要

• エントリーDOI: 10.2210/pdb2aps/pdb
• 分子名称: PROTEIN (CU,ZN SUPEROXIDE DISMUTASE), COPPER (II) ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: superoxide dismutase, sod, water-mediated dimer, beta barrel
• 由来する生物種: Actinobacillus pleuropneumoniae
• 細胞内の位置: Periplasm: P24702
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34893.74

構造登録者

Forest, K.T.,Langford, P.R.,Kroll, J.S.,Getzoff, E.D. (登録日: 1999-02-11, 公開日: 1999-02-25, 最終更新日: 2024-10-16)

主引用文献

Forest, K.T.,Langford, P.R.,Kroll, J.S.,Getzoff, E.D.
Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface.
J.Mol.Biol., 296:145-153, 2000

PubMed Abstract: Macrophages and neutrophils protect animals from microbial infection in part by issuing a burst of toxic superoxide radicals when challenged. To counteract this onslaught, many Gram-negative bacterial pathogens possess periplasmic Cu,Zn superoxide dismutases (SODs), which act on superoxide to yield molecular oxygen and hydrogen peroxide. We have solved the X-ray crystal structure of the Cu,Zn SOD from Actinobacillus pleuropneumoniae, a major porcine pathogen, by molecular replacement at 1.9 A resolution. The structure reveals that the dimeric bacterial enzymes form a structurally homologous class defined by a water-mediated dimer interface, and share with all Cu,Zn SODs the Greek-key beta-barrel subunit fold with copper and zinc ions located at the base of a deep loop-enclosed active-site channel. Our structure-based sequence alignment of the bacterial enzymes explains the monomeric nature of at least two of these, and suggests that there may be at least one additional structural class for the bacterial SODs. Two metal-mediated crystal contacts yielded our C222(1) crystals, and the geometry of these sites could be engineered into proteins recalcitrant to crystallization in their native form. This work highlights structural differences between eukaryotic and prokaryotic Cu,Zn SODs, as well as similarities and differences among prokaryotic SODs, and lays the groundwork for development of antimicrobial drugs that specifically target periplasmic Cu,Zn SODs of bacterial pathogens.

PubMed: 10656823
DOI: 10.1006/jmbi.1999.3448

実験手法

X-RAY DIFFRACTION (1.9 Å)