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TitleCryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states.
Journal, issue, pagesNat Struct Mol Biol, Vol. 24, Issue 12, Page 1146-1154, Year 2017
Publish dateNov 6, 2017
AuthorsXiaoyuan Zhou / Minghui Li / Deyuan Su / Qi Jia / Huan Li / Xueming Li / Jian Yang /
PubMed AbstractTRPML3 channels are mainly localized to endolysosomes and play a critical role in the endocytic pathway. Their dysfunction causes deafness and pigmentation defects in mice. TRPML3 activity is ...TRPML3 channels are mainly localized to endolysosomes and play a critical role in the endocytic pathway. Their dysfunction causes deafness and pigmentation defects in mice. TRPML3 activity is inhibited by low endolysosomal pH. Here we present cryo-electron microscopy (cryo-EM) structures of human TRPML3 in the closed, agonist-activated, and low-pH-inhibited states, with resolutions of 4.06, 3.62, and 4.65 Å, respectively. The agonist ML-SA1 lodges between S5 and S6 and opens an S6 gate. A polycystin-mucolipin domain (PMD) forms a luminal cap. S1 extends into this cap, forming a 'gating rod' that connects directly to a luminal pore loop, which undergoes dramatic conformational changes in response to low pH. S2 extends intracellularly and interacts with several intracellular regions to form a 'gating knob'. These unique structural features, combined with the results of electrophysiological studies, indicate a new mechanism by which luminal pH and other physiological modulators such as PIP regulate TRPML3 by changing S1 and S2 conformations.
External linksNat Struct Mol Biol / PubMed:29106414 / PubMed Central
MethodsEM (single particle)
Resolution3.62 - 4.65 Å
Structure data

7018

6aye

EMDB-7018, PDB-6aye:
Human apo-TRPML3 channel at pH 7.4
Method: EM (single particle) / Resolution: 4.06 Å

7019

6ayf

EMDB-7019, PDB-6ayf:
TRPML3/ML-SA1 complex at pH 7.4
Method: EM (single particle) / Resolution: 3.62 Å

7020

6ayg

EMDB-7020, PDB-6ayg:
Human Apo-TRPML3 channel at pH 4.8
Method: EM (single particle) / Resolution: 4.65 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / ion channel / TRP channel / lysosomal

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