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Catalytic Site Atlas

CSA LITERATURE entry for 1l7d

E.C. nameNAD(P)+ transhydrogenase (AB-specific)
SpeciesRhodospirillum rubrum (Bacteria)
E.C. Number (IntEnz) 1.6.1.2
CSA Homologues of 1l7d
CSA Entries With UniProtID Q2RSB2
CSA Entries With EC Number 1.6.1.2
PDBe Entry 1l7d
PDBSum Entry 1l7d
MACiE Entry 1l7d

Literature Report

IntroductionTranshydrogenase, isolated from Rhodospirillum rubrum, is a transmembrane protein that catalyses the hydride transfer from NADH to NADP+. The driving force for this reaction is the movement of a proton down a proton electrochemical gradient, with one proton transfer per hydride transfer, from the periplasm to the cytoplasm. Domain I (located in the pdb file) binds NADH and contains the catalytic residues for the reaction. Domain II facilitates proton translocation and domain III binds NADP+. Proton transfer through domain II propagates a conformational change from domain II through domain III to domain I. These conformational changes are required to align the substrates correctly and so couples proton translocation to hydride transfer.
MechansimUpon proton translocation conformational changes occur within all domains such that Arg127 of domain I is positioned to stabilise NADH in the proximal position. This allows NADH and NADP+ to align correctly and hydride transfer occurs between the C4 positions of the nicotinic rings of both substrates.
Reaction

Catalytic Sites for 1l7d

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA135135macie:sideChainAsp135 forms a hydrogen bond to Arg127 and stabilises the position of the latter to ensure the correct positioning of NADH. The hydrogen bond between the two residues is strengthened by hydrogen bonds between Asp135 and Ser138, and Asp135 and Gln132.
SerA138138macie:sideChainSer138 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.
ArgA127127macie:sideChainArg127 is positioned to stabilise the proximal position of NADH and allow hydride transfer. Arg127 is held in this position by a hydrogen bond to Asp135.
GlnA132132macie:sideChainGln132 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgB527127macie:sideChainArg127 is positioned to stabilise the proximal position of NADH and allow hydride transfer. Arg127 is held in this position by a hydrogen bond to Asp135.
GlnB532132macie:sideChainGln132 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.
SerB538138macie:sideChainSer138 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.
AspB535135macie:sideChainAsp135 forms a hydrogen bond to Arg127 and stabilises the position of the latter to ensure the correct positioning of NADH. The hydrogen bond between the two residues is strengthened by hydrogen bonds between Asp135 and Ser138, and Asp135 and Gln132.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
SerC938138macie:sideChainSer138 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.
GlnC932132macie:sideChainGln132 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.
AspC935135macie:sideChainAsp135 forms a hydrogen bond to Arg127 and stabilises the position of the latter to ensure the correct positioning of NADH. The hydrogen bond between the two residues is strengthened by hydrogen bonds between Asp135 and Ser138, and Asp135 and Gln132.
ArgC927127macie:sideChainArg127 is positioned to stabilise the proximal position of NADH and allow hydride transfer. Arg127 is held in this position by a hydrogen bond to Asp135.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspD1335135macie:sideChainAsp135 forms a hydrogen bond to Arg127 and stabilises the position of the latter to ensure the correct positioning of NADH. The hydrogen bond between the two residues is strengthened by hydrogen bonds between Asp135 and Ser138, and Asp135 and Gln132.
ArgD1327127macie:sideChainArg127 is positioned to stabilise the proximal position of NADH and allow hydride transfer. Arg127 is held in this position by a hydrogen bond to Asp135.
GlnD1332132macie:sideChainGln132 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.
SerD1338138macie:sideChainSer138 forms a hydrogen bond to Asp135, which strengthens the hydrogen bond between Asp135 and Arg127. This ensures that NADH is maintained in the proximal position.

Literature References

Notes:
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