Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum

被引：115

作者：

Newby, Zachary E. R. ^{[1
,2
,3
]}

O'Connell, Joseph, III ^{[1
,2
,3
]}

Robles-Colmenares, Yaneth ^{[1
,2
,3
]}

Khademi, Shahram ^{[1
,2
,3
]}

Miercke, Larry J. ^{[1
,2
,3
]}

Stroud, Robert M. ^{[1
,2
,3
]}

机构：

[1] Univ Calif San Francisco, Dept Chem, San Francisco, CA 94158 USA

[2] Univ Calif San Francisco, Chem Biol Grad Program, San Francisco, CA 94158 USA

[3] Univ Calif San Francisco, Sch Med, Dept Biochem & Biophys, San Francisco, CA 94158 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/nsmb.1431

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The 2.05-angstrom resolution structure of the aquaglyceroporin from the malarial parasite Plasmodium falciparum (PfAQP), a protein important in the parasite's life cycle, has been solved. The structure provides key evidence for the basis of water versus glycerol selectivity in aquaporin family members. Unlike its closest homolog of known structure, GlpF, the channel conducts both glycerol and water at high rates, framing the question of what determines high water conductance in aquaporin channels. The universally conserved arginine in the selectivity filter is constrained by only two hydrogen bonds in GlpF, whereas there are three in all water-selective aquaporins and in PfAQP. The decreased cost of dehydrating the triply-satisfied arginine cation may provide the basis for high water conductance. The two Asn-Pro-Ala (NPA) regions of PfAQP, which bear rare substitutions to Asn-Leu-Ala (NLA) and Asn-Pro-Ser (NPS), participate in preserving the orientation of the selectivity filter asparagines in the center of the channel.

引用

页码：619 / 625

页数：7

共 27 条

[21] Architecture and selectivity in aquaporins:: 2.5 Å X-ray structure of aquaporin Z [J].