葡萄糖凝固酶是辅因子诱导的生殖原体激活机制的原型
Rainer Friedrich1, Peter Panizzi, Pablo Fuentes-Prior
1Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany.
Nature
|October 3, 2003
概括
黄金葡萄球菌 (Staphylococcus aureus) 分泌葡萄球凝酶,这是一种新型的辅因子,直接激活人体前列血以启动血液凝结. 这种独特的机制,由晶体结构揭示,提供了细菌病原和zymogen激活的见解.
科学领域:
- 结构生物学是结构生物学.
- 微生物的病原发生.
- 生物化学 生物化学
背景情况:
- 细菌病原体经常分泌蛋白质来操纵宿主系统.
- 黄金葡萄球菌利用葡萄球凝聚酶激活血凝中的关键酶 - - 血栓激素.
研究的目的:
- 为了阐明稳定凝血酶介导的前激活的结构基础.
- 了解细菌辅因子直接激活生菌原的机制.
主要方法:
- 人类α-血栓和先血栓-2结合于稳定凝血酶的X射线晶体 (2.2 Å分辨率).
- 动力学研究评估了葡萄糖凝固酶N端的作用.
主要成果:
- 确定了与血/前血-2结合的葡萄凝聚酶的晶体结构,揭示了一个新的两域,三螺旋束折叠.
- 鉴定了稳定凝血酶的N端插入到前列-2-激活口袋中,诱导全激活.
- 证实了isoleucine 1和valine 2在稳定凝血酶活性中的关键作用.
结论:
- 葡萄糖凝固酶采用独特的"分子性"机制来激活生殖原体,与其他已知的激活剂不同.
- 新型葡萄糖凝固酶折叠在其他细菌毒性因子中得到保留.
- 结构性洞察力促进了对血液凝结和细菌病原性的理解.
相关概念视频
Cofactors and Coenzymes
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Enzymes
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Cofactors and Coenzymes
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Cofactors and Coenzymes
Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...


