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Preparation of a Corannulene-functionalized Hexahelicene by Copper(I)-catalyzed Alkyne-azide Cycloaddition of Nonplanar Polyaromatic Units
Published on: September 18, 2016
The structure of CorA: a Mg(2+)-selective channel
1Department of Pharmacology, Case School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4965, USA. mem6@po.cwru.edu
Current Opinion in Structural Biology
|July 11, 2006
Summary
The CorA Mg2+ transporter
Area of Science:
- Structural biology
- Biochemistry
- Molecular biology
Background:
- CorA is a magnesium transporter crucial for cellular function.
- Understanding its structure provides insights into ion transport mechanisms.
- This study completes structural data for major biological ion transporters.
Purpose of the Study:
- Determine the closed-form crystal structure of the CorA Mg2+ transporter from Thermatoga maritima.
- Characterize the structural features of CorA and compare them to other ion transporters.
- Elucidate the mechanism of Mg2+ transport by CorA.
Main Methods:
- X-ray crystallography
- Structural comparison
- Biochemical analysis
Main Results:
- The crystal structure of closed-form CorA was determined.
- CorA forms a funnel-shaped homopentamer with distinct membrane and cytoplasmic domains.
- Unusual features include periplasmic Mg2+ binding, a positive charge ring, and negatively charged cytosolic helices.
- Bound Mg2+ ions in the cytosolic domain appear to regulate transport.
Conclusions:
- The CorA structure reveals unique mechanisms for Mg2+ transport.
- Structural features suggest a novel gating mechanism involving charge interactions.
- This work provides a comprehensive understanding of biological magnesium transport.
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