3C02

X-ray structure of the aquaglyceroporin from Plasmodium falciparum

Summary for 3C02

• Entry DOI: 10.2210/pdb3c02/pdb
• Related: 1FX8
• Descriptor: Aquaglyceroporin, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• Functional Keywords: membrane protein, glycerol, water, transport, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, porin, transmembrane
• Biological source: Plasmodium falciparum (malaria parasite)
• Total number of polymer chains: 1
• Total formula weight: 29071.91

Authors

Newby, Z.E.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2008-01-18, release date: 2008-05-27, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.05 Å)