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Structure of Aquaporin Reveals Mechanism for Transport Selectivity

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Biochemists aren't much accustomed to seeing their work in the popular press, save for annual coverage of the Nobel prize in chemistry... Robert Stroud and colleagues recently solved the atomic structure of an aquaporin (GlpF) and have now solved the structure of another water channel from Escherichia coli, called aquaporin Z, that selectively conducts only water at high rates... Aquaporins form a large, diverse family of proteins and have been found in bacteria, plants, and animals... The high-resolution X-ray structures of recombinant aquaglyceroporin glycerol facilitator (GlpF)—a channel protein that transports both glycerol and water in E. coli—determined by the Stroud group in 2000 and of bovine aquaporin 1 (AQP1) from red blood cells, determined a year later, revealed how these aquaporins regulate their transport and selectivity... The aquaporin Z channel protein in E. coli can accommodate a flow of water at rates six times higher than GlpF, making it the prime subject for studying the selectivity of a high-conducting water channel... The architecture of aquaporin Z, the researchers report, is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel and amino acid side chains determining the size and chemistry of the channel... The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow... This structure confirms that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply can't fit... With two structural models of aquaporins down to the atomic level in the same species, scientists can now begin to investigate the molecular mechanisms that facilitate their selectivity... The importance of understanding these widely distributed channel proteins was underscored by the Nobel awards this year... Water transport is fundamental to life, and aquaporins are found throughout the body... Knowledge of their structure will help reveal the molecular mechanics of their specialized feats and promise to offer insights into a wide range of human disorders.

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Structure of aquaporin Z
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pbio.0000075-g001: Structure of aquaporin Z


Structure of Aquaporin Reveals Mechanism for Transport Selectivity
Structure of aquaporin Z
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC300685&req=5

pbio.0000075-g001: Structure of aquaporin Z

View Article: PubMed Central

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

Biochemists aren't much accustomed to seeing their work in the popular press, save for annual coverage of the Nobel prize in chemistry... Robert Stroud and colleagues recently solved the atomic structure of an aquaporin (GlpF) and have now solved the structure of another water channel from Escherichia coli, called aquaporin Z, that selectively conducts only water at high rates... Aquaporins form a large, diverse family of proteins and have been found in bacteria, plants, and animals... The high-resolution X-ray structures of recombinant aquaglyceroporin glycerol facilitator (GlpF)—a channel protein that transports both glycerol and water in E. coli—determined by the Stroud group in 2000 and of bovine aquaporin 1 (AQP1) from red blood cells, determined a year later, revealed how these aquaporins regulate their transport and selectivity... The aquaporin Z channel protein in E. coli can accommodate a flow of water at rates six times higher than GlpF, making it the prime subject for studying the selectivity of a high-conducting water channel... The architecture of aquaporin Z, the researchers report, is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel and amino acid side chains determining the size and chemistry of the channel... The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow... This structure confirms that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply can't fit... With two structural models of aquaporins down to the atomic level in the same species, scientists can now begin to investigate the molecular mechanisms that facilitate their selectivity... The importance of understanding these widely distributed channel proteins was underscored by the Nobel awards this year... Water transport is fundamental to life, and aquaporins are found throughout the body... Knowledge of their structure will help reveal the molecular mechanics of their specialized feats and promise to offer insights into a wide range of human disorders.

No MeSH data available.