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| | ==Crystal Structure of R. rubrum Transhydrogenase Domain I with Bound NADH== | | ==Crystal Structure of R. rubrum Transhydrogenase Domain I with Bound NADH== |
| - | <StructureSection load='1l7e' size='340' side='right' caption='[[1l7e]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1l7e' size='340' side='right'caption='[[1l7e]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1l7e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"dicrospirillum_rubrum"_enderlein_1925 "dicrospirillum rubrum" enderlein 1925]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1l7e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L7E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l7d|1l7d]], [[1f8g|1f8g]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(B-specific) NAD(P)(+) transhydrogenase (B-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.1 1.6.1.1] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7e OCA], [https://pdbe.org/1l7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l7e RCSB], [https://www.ebi.ac.uk/pdbsum/1l7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l7e ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7e OCA], [http://pdbe.org/1l7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l7e RCSB], [http://www.ebi.ac.uk/pdbsum/1l7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l7e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PNTAA_RHORU PNTAA_RHORU]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity). | + | [https://www.uniprot.org/uniprot/PNTAA_RHORT PNTAA_RHORT] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.[UniProtKB:P07001] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1l7e" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1l7e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dicrospirillum rubrum enderlein 1925]] | + | [[Category: Large Structures]] |
| - | [[Category: Hatefi, Y]] | + | [[Category: Rhodospirillum rubrum]] |
| - | [[Category: Prasad, G S]] | + | [[Category: Hatefi Y]] |
| - | [[Category: Sridhar, V]] | + | [[Category: Prasad GS]] |
| - | [[Category: Stout, C D]] | + | [[Category: Sridhar V]] |
| - | [[Category: Wahlberg, M]] | + | [[Category: Stout CD]] |
| - | [[Category: Yamaguchi, M]] | + | [[Category: Wahlberg M]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Yamaguchi M]] |
| - | [[Category: Transhydrogenase domain i with nadh bound]]
| + | |
| Structural highlights
Function
PNTAA_RHORT The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.[UniProtKB:P07001]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Transhydrogenase (TH) is a dimeric integral membrane enzyme in mitochondria and prokaryotes that couples proton translocation across a membrane with hydride transfer between NAD(H) and NADP(H) in soluble domains. Crystal structures of the NAD(H) binding alpha1 subunit (domain I) of Rhodospirillum rubrum TH have been determined at 1.8 A resolution in the absence of dinucleotide and at 1.9 A resolution with NADH bound. Each structure contains two domain I dimers in the asymmetric unit (AB and CD); the dimers are intimately associated and related by noncrystallographic 2-fold axes. NADH binds to subunits A and D, consistent with the half-of-the-sites reactivity of the enzyme. The conformation of NADH in subunits A and D is very similar; the nicotinamide is in the anti conformation, the A-face is exposed to solvent, and both N7 and O7 participate in hydrogen bonds. Comparison of subunits A and D to six independent copies of the subunit without bound NADH reveals multiple conformations for residues and loops surrounding the NADH site, indicating flexibility for binding and release of the substrate (product). The NADH-bound structure is also compared to the structures of R. rubrum domain I with NAD bound (PDB code 1F8G) and with NAD bound in complex with domain III of TH (PDB code 1HZZ). The NADH- vs NAD-bound domain I structures reveal conformational differences in conserved residues in the NAD(H) binding site and in dinucleotide conformation that are correlated with the net charge, i.e., oxidation state, of the nicotinamides. The comparisons illustrate how nicotinamide oxidation state can affect the domain I conformation, which is relevant to the hydride transfer step of the overall reaction.
Crystal structures of transhydrogenase domain I with and without bound NADH.,Prasad GS, Wahlberg M, Sridhar V, Sundaresan V, Yamaguchi M, Hatefi Y, Stout CD Biochemistry. 2002 Oct 22;41(42):12745-54. PMID:12379117[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Prasad GS, Wahlberg M, Sridhar V, Sundaresan V, Yamaguchi M, Hatefi Y, Stout CD. Crystal structures of transhydrogenase domain I with and without bound NADH. Biochemistry. 2002 Oct 22;41(42):12745-54. PMID:12379117
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