1ptj
From Proteopedia
(New page: 200px<br /><applet load="1ptj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ptj, resolution 2.61Å" /> '''Crystal structure an...) |
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| - | [[Image:1ptj.jpg|left|200px]]<br /><applet load="1ptj" size=" | + | [[Image:1ptj.jpg|left|200px]]<br /><applet load="1ptj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ptj, resolution 2.61Å" /> | caption="1ptj, resolution 2.61Å" /> | ||
'''Crystal structure analysis of the DI and DIII complex of transhydrogenase with a thio-nicotinamide nucleotide analogue'''<br /> | '''Crystal structure analysis of the DI and DIII complex of transhydrogenase with a thio-nicotinamide nucleotide analogue'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transhydrogenase couples the reduction of NADP+ by NADH to inward proton | + | Transhydrogenase couples the reduction of NADP+ by NADH to inward proton translocation across mitochondrial and bacterial membranes. The coupling reactions occur within the protein by long distance conformational changes. In intact transhydrogenase and in complexes formed from the isolated, nucleotide-binding components, thio-NADP(H) is a good analogue for NADP(H), but thio-NAD(H) is a poor analogue for NAD(H). Crystal structures of the nucleotide-binding components show that the twists of the 3-carbothiamide groups of thio-NADP+ and of thio-NAD+ (relative to the planes of the pyridine rings), which are defined by the dihedral, Xam, are altered relative to the twists of the 3-carboxamide groups of the physiological nucleotides. The finding that thio-NADP+ is a good substrate despite an increased Xam value shows that approach of the NADH prior to hydride transfer is not obstructed by the S atom in the analogue. That thio-NAD(H) is a poor substrate appears to be the result of failure in the conformational change that establishes the ground state for hydride transfer. This might be a consequence of restricted rotation of the 3-carbothiamide group during the conformational change. |
==About this Structure== | ==About this Structure== | ||
| - | 1PTJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with SND, NAP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1PTJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with <scene name='pdbligand=SND:'>SND</scene>, <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodospirillum rubrum]] | [[Category: Rhodospirillum rubrum]] | ||
| - | [[Category: Boxel, G | + | [[Category: Boxel, G I.van.]] |
| - | [[Category: Jackson, J | + | [[Category: Jackson, J B.]] |
| - | [[Category: Quirk, P | + | [[Category: Quirk, P G.]] |
| - | [[Category: Rodrigues, D | + | [[Category: Rodrigues, D J.]] |
[[Category: Singh, A.]] | [[Category: Singh, A.]] | ||
| - | [[Category: Venning, J | + | [[Category: Venning, J D.]] |
| - | [[Category: White, S | + | [[Category: White, S A.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: NAP]] | [[Category: NAP]] | ||
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[[Category: transhydrogenase]] | [[Category: transhydrogenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:24 2008'' |
Revision as of 12:32, 21 February 2008
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Crystal structure analysis of the DI and DIII complex of transhydrogenase with a thio-nicotinamide nucleotide analogue
Overview
Transhydrogenase couples the reduction of NADP+ by NADH to inward proton translocation across mitochondrial and bacterial membranes. The coupling reactions occur within the protein by long distance conformational changes. In intact transhydrogenase and in complexes formed from the isolated, nucleotide-binding components, thio-NADP(H) is a good analogue for NADP(H), but thio-NAD(H) is a poor analogue for NAD(H). Crystal structures of the nucleotide-binding components show that the twists of the 3-carbothiamide groups of thio-NADP+ and of thio-NAD+ (relative to the planes of the pyridine rings), which are defined by the dihedral, Xam, are altered relative to the twists of the 3-carboxamide groups of the physiological nucleotides. The finding that thio-NADP+ is a good substrate despite an increased Xam value shows that approach of the NADH prior to hydride transfer is not obstructed by the S atom in the analogue. That thio-NAD(H) is a poor substrate appears to be the result of failure in the conformational change that establishes the ground state for hydride transfer. This might be a consequence of restricted rotation of the 3-carbothiamide group during the conformational change.
About this Structure
1PTJ is a Protein complex structure of sequences from Rhodospirillum rubrum with , and as ligands. Active as NAD(P)(+) transhydrogenase (AB-specific), with EC number 1.6.1.2 Full crystallographic information is available from OCA.
Reference
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., Singh A, Venning JD, Quirk PG, van Boxel GI, Rodrigues DJ, White SA, Jackson JB, J Biol Chem. 2003 Aug 29;278(35):33208-16. Epub 2003 Jun 5. PMID:12791694
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