2fr8: Difference between revisions
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[[Image:2fr8.gif|left|200px]] | [[Image:2fr8.gif|left|200px]] | ||
'''Structure of transhydrogenase (dI.R127A.NAD+)2(dIII.NADP+)1 asymmetric complex''' | {{Structure | ||
|PDB= 2fr8 |SIZE=350|CAPTION= <scene name='initialview01'>2fr8</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(AB-specific) NAD(P)(+) transhydrogenase (AB-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] | |||
|GENE= pntAA, nntA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 Rhodospirillum rubrum]), pntB, nntB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 Rhodospirillum rubrum]) | |||
}} | |||
'''Structure of transhydrogenase (dI.R127A.NAD+)2(dIII.NADP+)1 asymmetric complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FR8 is a [ | 2FR8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FR8 OCA]. | ||
==Reference== | ==Reference== | ||
The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase., Brondijk TH, van Boxel GI, Mather OC, Quirk PG, White SA, Jackson JB, J Biol Chem. 2006 May 12;281(19):13345-54. Epub 2006 Mar 13. PMID:[http:// | The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase., Brondijk TH, van Boxel GI, Mather OC, Quirk PG, White SA, Jackson JB, J Biol Chem. 2006 May 12;281(19):13345-54. Epub 2006 Mar 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16533815 16533815] | ||
[[Category: NAD(P)(+) transhydrogenase (AB-specific)]] | [[Category: NAD(P)(+) transhydrogenase (AB-specific)]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: NAD]] | [[Category: NAD]] | ||
[[Category: NAP]] | [[Category: NAP]] | ||
[[Category: nad(p) transhydrogenase | [[Category: nad(p) transhydrogenase subunit]] | ||
[[Category: nad+]] | [[Category: nad+]] | ||
[[Category: nadp+]] | [[Category: nadp+]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:55:50 2008'' | ||
Revision as of 17:55, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | pntAA, nntA1 (Rhodospirillum rubrum), pntB, nntB (Rhodospirillum rubrum) | ||||||
| Activity: | NAD(P)(+) transhydrogenase (AB-specific), with EC number 1.6.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of transhydrogenase (dI.R127A.NAD+)2(dIII.NADP+)1 asymmetric complex
OverviewOverview
Transhydrogenase couples proton translocation across a membrane to hydride transfer between NADH and NADP+. Previous x-ray structures of complexes of the nucleotide-binding components of transhydrogenase ("dI2dIII1" complexes) indicate that the dihydronicotinamide ring of NADH can move from a distal position relative to the nicotinamide ring of NADP+ to a proximal position. The movement might be responsible for gating hydride transfer during proton translocation. We have mutated three invariant amino acids, Arg-127, Asp-135, and Ser-138, in the NAD(H)-binding site of Rhodospirillum rubrum transhydrogenase. In each mutant, turnover by the intact enzyme is strongly inhibited. Stopped-flow experiments using dI2dIII1 complexes show that inhibition results from a block in the steps associated with hydride transfer. Mutation of Asp-135 and Ser-138 had no effect on the binding affinity of either NAD+ or NADH, but mutation of Arg-127 led to much weaker binding of NADH and slightly weaker binding of NAD+. X-ray structures of dI2dIII1 complexes carrying the mutations showed that their effects were restricted to the locality of the bound NAD(H). The results are consistent with the suggestion that in wild-type protein movement of the Arg-127 side chain, and its hydrogen bonding to Asp-135 and Ser-138, stabilizes the dihydronicotinamide of NADH in the proximal position for hydride transfer.
About this StructureAbout this Structure
2FR8 is a Protein complex structure of sequences from Rhodospirillum rubrum. Full crystallographic information is available from OCA.
ReferenceReference
The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase., Brondijk TH, van Boxel GI, Mather OC, Quirk PG, White SA, Jackson JB, J Biol Chem. 2006 May 12;281(19):13345-54. Epub 2006 Mar 13. PMID:16533815
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