3.D.2.2.2 H+-transporting NADH/NADP Transhydrogenase, PntA1 (α1)/PntA2 (α2)/PntB (β). A 3-d structure is available (Leung et al. 2015). Another structre (2.2 Å resolution) revealed conformational changes of helix positions from the previous structure solved at pH 8.5, and internal water molecules interacting with residues implicated in proton translocation. Water flows across a narrow pore and a hydrophobic "dry" region in the middle of the membrane channel, with key residues His42alpha2 (chain A) being protonated and Thr214beta (chain B) displaying a conformational change, respectively, to gate the channel access to both cytoplasmic and periplasmic chambers. Mutation of Thr214beta to Ala deactivated the enzyme (Padayatti et al. 2017).
|
Accession Number: | Q72GS0 |
Protein Name: | NAD(P) transhydrogenase subunit beta |
Length: | 450 |
Molecular Weight: | 47336.00 |
Species: | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [262724] |
Number of TMSs: | 9 |
Substrate |
hydron |
---|
1: MDLIQAAYFV VAILFIVGLK RMAHPTTAKS GIVWAGWGMV LAVLATFFWP GMGNFALILL
61: ALLLGSVVAW WAAVRVAMTD MPQMVAIYNG MGGGAAATIA AVELLKGAFE NTGLMALAIL
121: GGLIGSVAFT GSLIAFAKLQ GIMKSRPILF PGQKAVNALV LALTVVIGLS LLWNDATASI
181: VLFFLLALLF GVLMTLPIGG GDMPVAISFY NAFTGMAVGF EGFAVGNPAL MVAGTLVGAA
241: GTLLTVLMAR AMNRSVWSVL VGGFGVEQEA GEVKGSLKPI DVEDAAVMLA YAGKVVFVPG
301: YGMALSQAQH KLKELADLLE ARGVEVKFAI HPVAGRMPGH MNVLLAEAGV DYDKLKDLEE
361: INPEFPTVDV AVVIGANDVV NPAARRPGSP LYGMPILDVD KAKNVIVIKR GQGKGFAGVE
421: NELFYAENTR MLYGDAQKVL TELIQALKRL