PDBsum entry 1e3t

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Transhydrogenase PDB id
Protein chain
175 a.a. *
* Residue conservation analysis
PDB id:
Name: Transhydrogenase
Title: Solution structure of the NADP(h) binding component (diii) of proton-translocating transhydrogenase from rhodospirillum rubrum
Structure: Nicotinamide nucleotide transhydrogenase (subunit beta). Chain: a. Fragment: NADP(h) binding domain. Synonym: diii, NAD(p)(+) transhydrogenase (b-specific), pyridine nucleotide transhydrogenase. Engineered: yes
Source: Rhodospirillum rubrum. Organism_taxid: 1085. Gene: pntb. Expressed in: escherichia coli. Expression_system_taxid: 469008.
NMR struc: 1 models
Authors: M.Jeeves,K.J.Smith,P.G.Quirk,N.P.J.Cotton,J.B.Jackson
Key ref: M.Jeeves et al. (2000). Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum. Biochim Biophys Acta, 1459, 248-257. PubMed id: 11004437 DOI: 10.1016/S0005-2728(00)00159-6
22-Jun-00     Release date:   03-Oct-00    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q2RSB4  (PNTB_RHORT) -  NAD(P) transhydrogenase subunit beta
464 a.a.
175 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - NAD(P)(+) transhydrogenase (Re/Si-specific).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: NADPH + NAD+ = NADP+ + NADH
Bound ligand (Het Group name = NAP)
corresponds exactly
+ NAD(+)
= NADP(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     integral to membrane   1 term 
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     NADP binding     2 terms  


DOI no: 10.1016/S0005-2728(00)00159-6 Biochim Biophys Acta 1459:248-257 (2000)
PubMed id: 11004437  
Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum.
M.Jeeves, K.J.Smith, P.G.Quirk, N.P.Cotton, J.B.Jackson.
Transhydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, 21.5 kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods. This is the first description of the structure of dIII from a bacterial source. The protein adopts a Rossmann fold: an open, twisted, parallel beta-sheet, flanked by helices. However, the binding of NADP(+) to dIII is profoundly different to that seen in other Rossmann structures, in that its orientation is reversed: the adenosine moiety interacts with the first betaalphabetaalphabeta motif, and the nicotinamide with the second. Features in the structure that might be responsible for changes in nucleotide-binding affinity during catalysis, and for interaction with other components of the enzyme, are identified. The results are compared with the recently determined, high-resolution crystal structures of human and bovine dIII which also show the reversed nucleotide orientation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18972197 A.Pedersen, G.B.Karlsson, and J.Rydström (2008).
Proton-translocating transhydrogenase: an update of unsolved and controversial issues.
  J Bioenerg Biomembr, 40, 463-473.  
15039572 C.Oswald, T.Johansson, S.Törnroth, M.Okvist, and U.Krengel (2004).
Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase.
  Acta Crystallogr D Biol Crystallogr, 60, 743-745.  
12791694 A.Singh, J.D.Venning, P.G.Quirk, G.I.van Boxel, D.J.Rodrigues, S.A.White, and J.B.Jackson (2003).
Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation.
  J Biol Chem, 278, 33208-33216.
PDB codes: 1pt9 1ptj
14567675 V.Sundaresan, M.Yamaguchi, J.Chartron, and C.D.Stout (2003).
Conformational change in the NADP(H) binding domain of transhydrogenase defines four states.
  Biochemistry, 42, 12143-12153.
PDB codes: 1pno 1pnq
12230562 C.Johansson, A.Pedersen, B.G.Karlsson, and J.Rydström (2002).
Redox-sensitive loops D and E regulate NADP(H) binding in domain III and domain I-domain III interactions in proton-translocating Escherichia coli transhydrogenase.
  Eur J Biochem, 269, 4505-4515.  
11231296 D.J.Rodrigues, J.D.Venning, P.G.Quirk, and J.B.Jackson (2001).
A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release.
  Eur J Biochem, 268, 1430-1438.  
11250201 N.P.Cotton, S.A.White, S.J.Peake, S.McSweeney, and J.B.Jackson (2001).
The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase.
  Structure, 9, 165-176.
PDB code: 1hzz
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.