| 000 | 02369 am a22003733u 4500 | ||
|---|---|---|---|
| 042 | _adc | ||
| 100 | 1 | 0 |
_aChoi, Hyun-Kyu _eauthor _91112 |
| 700 | 1 | 0 |
_aKang, Hyunook _eauthor _91113 |
| 700 | 1 | 0 |
_aLee, Chanwoo _eauthor _91114 |
| 700 | 1 | 0 |
_aKim, Hyun Gyu _eauthor _91115 |
| 700 | 1 | 0 |
_aPhillips, Ben P. _eauthor _91116 |
| 700 | 1 | 0 |
_aPark, Soohyung _eauthor _91117 |
| 700 | 1 | 0 |
_aTumescheit, Charlotte _eauthor _91118 |
| 700 | 1 | 0 |
_aKim, Sang Ah _eauthor _91119 |
| 700 | 1 | 0 |
_aLee, Hansol _eauthor _91120 |
| 700 | 1 | 0 |
_aRoh, Soung-Hun _eauthor _91121 |
| 700 | 1 | 0 |
_aHong, Heedeok _eauthor _91122 |
| 700 | 1 | 0 |
_aSteinegger, Martin _eauthor _91123 |
| 700 | 1 | 0 |
_aIm, Wonpil _eauthor _91124 |
| 700 | 1 | 0 |
_aMiller, Elizabeth A. _eauthor _91125 |
| 700 | 1 | 0 |
_aChoi, Hee-Jung _eauthor _91126 |
| 700 | 1 | 0 |
_aYoon, Tae-Young _eauthor _91127 |
| 245 | 0 | 0 | _aEvolutionary balance between foldability and functionality of a glucose transporter |
| 260 | _c2022-07-01. | ||
| 500 | _a/pmc/articles/PMC7612945/ | ||
| 500 | _a/pubmed/35484435 | ||
| 520 | _aDespite advances in resolving structures of multi-pass membrane proteins, little is known about the native folding pathways of these complex structures. Using single-molecule magnetic tweezers, we here report a folding pathway of purified human glucose transporter 3 (GLUT3) reconstituted within synthetic lipid bilayers. The N-terminal major facilitator superfamily (MFS) fold strictly forms first, serving as structural templates for its C-terminal counterpart, in which polar residues comprising the conduit for glucose molecules present major folding challenges. The ER membrane protein complex facilitates insertion of these hydrophilic transmembrane helices, thrusting GLUT3's microstate sampling toward folded structures. Final assembly between the N- and C-terminal MFS folds depends on specific lipids that ease desolvation of lipid shells surrounding the domain interfaces. Sequence analysis suggests that this asymmetric folding propensity across the N-and C-terminal MFS folds prevails for metazoan sugar porters, revealing evolutionary conflicts between foldability and functionality faced by many multi-pass membrane proteins. | ||
| 540 | _a | ||
| 546 | _aen | ||
| 690 | _aArticle | ||
| 655 | 7 |
_aText _2local |
|
| 786 | 0 | _nNat Chem Biol | |
| 856 | 4 | 1 |
_uhttp://dx.doi.org/10.1038/s41589-022-01002-w _zConnect to this object online. |
| 999 |
_c1840 _d1840 |
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