8amw | pdb_00008amw

AQP7 dimer of tetramers_C1

Structural highlights

8amw is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	GOL
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AQP7_HUMAN Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (PubMed:9405233, PubMed:11952783, PubMed:30423801, PubMed:30420639). The channel is also permeable to urea (PubMed:9405233). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity).[UniProtKB:O54794]^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 A resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic alpha- and beta- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.

Cryo-EM structure supports a role of AQP7 as a junction protein.,Huang P, Venskutonyte R, Prasad RB, Ardalani H, de Mare SW, Fan X, Li P, Spegel P, Yan N, Gourdon P, Artner I, Lindkvist-Petersson K Nat Commun. 2023 Feb 3;14(1):600. doi: 10.1038/s41467-023-36272-y. PMID:36737436^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kondo H, Shimomura I, Kishida K, Kuriyama H, Makino Y, Nishizawa H, Matsuda M, Maeda N, Nagaretani H, Kihara S, Kurachi Y, Nakamura T, Funahashi T, Matsuzawa Y. Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation. Eur J Biochem. 2002 Apr;269(7):1814-26. doi: 10.1046/j.1432-1033.2002.02821.x. PMID:11952783 doi:https://dx.doi.org/10.1046/j.1432-1033.2002.02821.x
↑ Gotfryd K, Mosca AF, Missel JW, Truelsen SF, Wang K, Spulber M, Krabbe S, Helix-Nielsen C, Laforenza U, Soveral G, Pedersen PA, Gourdon P. Human adipose glycerol flux is regulated by a pH gate in AQP10. Nat Commun. 2018 Nov 12;9(1):4749. doi: 10.1038/s41467-018-07176-z. PMID:30420639 doi:https://dx.doi.org/10.1038/s41467-018-07176-z
↑ Mosca AF, de Almeida A, Wragg D, Martins AP, Sabir F, Leoni S, Moura TF, Prista C, Casini A, Soveral G. Molecular Basis of Aquaporin-7 Permeability Regulation by pH. Cells. 2018 Nov 10;7(11). pii: cells7110207. doi: 10.3390/cells7110207. PMID:30423801 doi:https://dx.doi.org/10.3390/cells7110207
↑ Kuriyama H, Kawamoto S, Ishida N, Ohno I, Mita S, Matsuzawa Y, Matsubara K, Okubo K. Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability. Biochem Biophys Res Commun. 1997 Dec 8;241(1):53-8. doi: 10.1006/bbrc.1997.7769. PMID:9405233 doi:https://dx.doi.org/10.1006/bbrc.1997.7769
↑ Huang P, Venskutonytė R, Prasad RB, Ardalani H, de Maré SW, Fan X, Li P, Spégel P, Yan N, Gourdon P, Artner I, Lindkvist-Petersson K. Cryo-EM structure supports a role of AQP7 as a junction protein. Nat Commun. 2023 Feb 3;14(1):600. PMID:36737436 doi:10.1038/s41467-023-36272-y

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OCA

[1] Kondo H, Shimomura I, Kishida K, Kuriyama H, Makino Y, Nishizawa H, Matsuda M, Maeda N, Nagaretani H, Kihara S, Kurachi Y, Nakamura T, Funahashi T, Matsuzawa Y. Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation. Eur J Biochem. 2002 Apr;269(7):1814-26. doi: 10.1046/j.1432-1033.2002.02821.x. PMID:11952783 doi:https://dx.doi.org/10.1046/j.1432-1033.2002.02821.x

[2] Gotfryd K, Mosca AF, Missel JW, Truelsen SF, Wang K, Spulber M, Krabbe S, Helix-Nielsen C, Laforenza U, Soveral G, Pedersen PA, Gourdon P. Human adipose glycerol flux is regulated by a pH gate in AQP10. Nat Commun. 2018 Nov 12;9(1):4749. doi: 10.1038/s41467-018-07176-z. PMID:30420639 doi:https://dx.doi.org/10.1038/s41467-018-07176-z

[3] Mosca AF, de Almeida A, Wragg D, Martins AP, Sabir F, Leoni S, Moura TF, Prista C, Casini A, Soveral G. Molecular Basis of Aquaporin-7 Permeability Regulation by pH. Cells. 2018 Nov 10;7(11). pii: cells7110207. doi: 10.3390/cells7110207. PMID:30423801 doi:https://dx.doi.org/10.3390/cells7110207

[4] Kuriyama H, Kawamoto S, Ishida N, Ohno I, Mita S, Matsuzawa Y, Matsubara K, Okubo K. Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability. Biochem Biophys Res Commun. 1997 Dec 8;241(1):53-8. doi: 10.1006/bbrc.1997.7769. PMID:9405233 doi:https://dx.doi.org/10.1006/bbrc.1997.7769

[5] Huang P, Venskutonytė R, Prasad RB, Ardalani H, de Maré SW, Fan X, Li P, Spégel P, Yan N, Gourdon P, Artner I, Lindkvist-Petersson K. Cryo-EM structure supports a role of AQP7 as a junction protein. Nat Commun. 2023 Feb 3;14(1):600. PMID:36737436 doi:10.1038/s41467-023-36272-y

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8amw | pdb_00008amw

AQP7 dimer of tetramers_C1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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