3C02

X-ray structure of the aquaglyceroporin from Plasmodium falciparum

3C02 の概要

• エントリーDOI: 10.2210/pdb3c02/pdb
• 関連するPDBエントリー: 1FX8
• 分子名称: Aquaglyceroporin, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: membrane protein, glycerol, water, transport, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, porin, transmembrane
• 由来する生物種: Plasmodium falciparum (malaria parasite)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29071.91

構造登録者

Newby, Z.E.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (登録日: 2008-01-18, 公開日: 2008-05-27, 最終更新日: 2023-08-30)

主引用文献

Newby, Z.E.,O'Connell, J.,Robles-Colmenares, Y.,Khademi, S.,Miercke, L.J.,Stroud, R.M.
Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum.
Nat.Struct.Mol.Biol., 15:619-625, 2008

PubMed Abstract: The 2.05-A 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.

PubMed: 18500352
DOI: 10.1038/nsmb.1431

実験手法

X-RAY DIFFRACTION (2.05 Å)