2.A.55.3.7 H+-stimulated, divalent metal cation uptake system, MntH of 436 aas and 11 TMSs. The x-ray structure has been determined, revealing the probable ion translocation pathway (Bozzi et al. 2016). Metal ion and
proton may enter the transporter via the same external pathway to the ir
binding sites, but they follow separate routes to the cytoplasm, which could
facilitate the co-transport of two cationic species (Bozzi et al. 2019). The results
illustrate the flexibility of the LeuT fold to support a broad range of
substrate transport and conformational change mechanisms. Transmembrane helix 6b links proton- and metal-release pathways and drives conformational changes (Bozzi et al. 2019).
|
Accession Number: | Q9RTP8 |
Protein Name: | Divalent metal cation transporter MntH |
Length: | 436 |
Molecular Weight: | 46652.00 |
Species: | Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [243230] |
Number of TMSs: | 11 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
metal cation, hydron |
---|
1: MDSRSPSLPD DRPDPPEQHL DARAGATLRG TAGPRGVRRI LPFLGPAVIA SIAYMDPGNF
61: ATNIEGGARY GYSLLWVILA ANLMAMVIQN LSANLGIASG RNLPELIRER WPRPLVWFYW
121: IQAELVAMAT DLAEFLGAAL AIQLLTGLPM FWGAVVTGVV TFWLLNLQKR GTRPLELAVG
181: AFVLMIGVAY LVQVVLARPD LAAVGAGFVP RLQGPGSAYL AVGIIGATVM PHVIYLHSAL
241: TQGRIQTDTT EEKRRLVRLN RVDVIAAMGL AGLINMSMLA VAAATFHGKN VENAGDLTTA
301: YQTLTPLLGP AASVLFAVAL LASGLSSSAV GTMAGDVIMQ GFMGFHIPLW LRRLITMLPA
361: FIVILLGMDP SSVLILSQVI LCFGVPFALV PLLLFTARRD VMGALVTRRS FTVIGWVIAV
421: IIIALNGYLL WELLGG