1.A.8.6.3
Aquaporin, Aqy1 (PIP2-7 7). The subangstron (0.88Å) structure is available (Kosinska Eriksson et al. 2013). the H-bond donor interactions of the NPA motif''s asparagine residues to
passing water molecules are revealed. A polarized water-water H-bond
configuration is observed within the channel. Four selectivity filter water positions
are too closely spaced to be simultaneously occupied. Strongly correlated
movements break the connectivity of selectivity filter water molecules to other water molecules
within the channel, thereby preventing proton transport via a Grotthuss
mechanism.
|
Accession Number: | F2QVG4 |
Protein Name: | Aquaporin PIP2-7 7 |
Length: | 279 |
Molecular Weight: | 29915.00 |
Species: | Komagataella pastoris (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1) (Yeast) [981350] |
Number of TMSs: | 6 |
Substrate |
water |
---|
1: MPDIENQAAD GQAEIKPEDA PYITNAYKPA YARWGFGSDS VRNHFIAMSG EFVGTFLFLW
61: SAFVIAQIAN QAPETPDGGS NPAQLIMISF GFGFGVMVGV FITYRVSGGN LNPAVTLALV
121: LARAIPPFRG ILMAFTQIVA GMAAAGAASA MTPGEIAFAN ALGGGASRTR GLFLEAFGTA
181: ILCLTVLMLA VEKHRATWFA PFVIGIALLI AHLICIYYTG AGLNPARSFG PAVAARSFPN
241: YHWIYWLGPI LGAFLAYSIW QMWKWLNYQT TNPGQDSDA