• 主页
  • 查找结果
  • Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense.

Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense.

Proceedings of the National Academy of Sciences of the United States of America (2014-04-09)
Julie E Gleason, Ahmad Galaleldeen, Ryan L Peterson, Alexander B Taylor, Stephen P Holloway, Jessica Waninger-Saroni, Brendan P Cormack, Diane E Cabelli, P John Hart, Valeria Cizewski Culotta
摘要

The human fungal pathogens Candida albicans and Histoplasma capsulatum have been reported to protect against the oxidative burst of host innate immune cells using a family of extracellular proteins with similarity to Cu/Zn superoxide dismutase 1 (SOD1). We report here that these molecules are widespread throughout fungi and deviate from canonical SOD1 at the primary, tertiary, and quaternary levels. The structure of C. albicans SOD5 reveals that although the β-barrel of Cu/Zn SODs is largely preserved, SOD5 is a monomeric copper protein that lacks a zinc-binding site and is missing the electrostatic loop element proposed to promote catalysis through superoxide guidance. Without an electrostatic loop, the copper site of SOD5 is not recessed and is readily accessible to bulk solvent. Despite these structural deviations, SOD5 has the capacity to disproportionate superoxide with kinetics that approach diffusion limits, similar to those of canonical SOD1. In cultures of C. albicans, SOD5 is secreted in a disulfide-oxidized form and apo-pools of secreted SOD5 can readily capture extracellular copper for rapid induction of enzyme activity. We suggest that the unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface.

材料
货号
品牌
产品描述

Sigma-Aldrich
铜, powder, <425 μm, 99.5% trace metals basis
Sigma-Aldrich
铜, powder, 99.999% trace metals basis
Sigma-Aldrich
铜, foil, thickness 0.25 mm, 99.98% trace metals basis
Sigma-Aldrich
铜, wire, diam. 1.0 mm, ≥99.9%
Sigma-Aldrich
铜, powder, <75 μm, 99%
Sigma-Aldrich
铜, powder (spheroidal), 10-25 μm, 98%
Sigma-Aldrich
铜, ACS reagent, granular, 10-40 mesh, ≥99.90%
Sigma-Aldrich
铜, nanopowder, 60-80 nm particle size (SAXS), ≥99.5% trace metals basis
Sigma-Aldrich
铜, nanopowder, 40-60 nm particle size (SAXS), ≥99.5% trace metals basis
Sigma-Aldrich
铜, electrolytic, Analytical Reagent, reag. Ph. Eur., ≥99.9% (complexometric), wire
Sigma-Aldrich
铜, foil, thickness 0.025 mm, 99.98% trace metals basis
Sigma-Aldrich
铜, foil, thickness 1.0 mm, 99.999% trace metals basis
Sigma-Aldrich
铜, powder (dendritic), <45 μm, 99.7% trace metals basis
Sigma-Aldrich
铜, foil, thickness 0.5 mm, 99.98% trace metals basis
Sigma-Aldrich
铜, turnings, purum p.a., ≥99.0%
Sigma-Aldrich
铜, foil, ≥99.8% (complexometric)
Sigma-Aldrich
铜, wire, diam. 0.25 mm, 99.999% trace metals basis
Sigma-Aldrich
铜, beads, 2-8 mm, ≥99.99% trace metals basis
Sigma-Aldrich
铜, beads, 2-8 mm, 99.9995% trace metals basis
Sigma-Aldrich
铜, wire, diam. 2.0 mm, 99.999% trace metals basis
Sigma-Aldrich
铜, wire, diam. 0.64 mm, 99.995% trace metals basis
铜, foil, 150x150mm, thickness 0.20mm, hard, 99.95+%
铜, wire reel, 100m, diameter 0.05mm, annealed, 99.9%
铜, wire reel, 1000m, diameter 0.1mm, annealed, 99.9%
铜, wire reel, 5m, diameter 0.025mm, as drawn, 99.99+%
铜, wire reel, 1000m, diameter 0.125mm, annealed, 99.9%
铜, foil, 150x150mm, thickness 0.125mm, hard, 99.95+%
铜, rod, 100mm, diameter 4.8mm, hard, 99.9%
铜, tube, 100mm, outside diameter 2.0mm, inside diameter 1.6mm, wall thickness 0.2mm, as drawn, 99.9%
铜, tube, 100mm, outside diameter 2.5mm, inside diameter 1.9mm, wall thickness 0.3mm, as drawn, 99.9%

社交媒体

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

Merck

科研、开发、生产。

作为生命科学行业的全球领先供应商,我们致力于为科研、生物技术开发和生产,以及制药药物疗法开发和生产提供各类解决方案和服务。

© 2021年版权归德国达姆施塔特默克集团(Merck KGaA)及/或其附属公司所有。版权所有。

未经许可,严禁复制本网站上的任何资料。