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< | ==Solution Structure of the NADP(H) binding Component (dIII) of Proton-Translocating Transhydrogenase from Rhodospirillum rubrum== | ||
<StructureSection load='1e3t' size='340' side='right'caption='[[1e3t]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E3T FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=1e3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3t OCA], [https://pdbe.org/1e3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e3t RCSB], [https://www.ebi.ac.uk/pdbsum/1e3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e3t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PNTB_RHORT PNTB_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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e3t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e3t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum.,Jeeves M, Smith KJ, Quirk PG, Cotton NP, Jackson JB Biochim Biophys Acta. 2000 Aug 15;1459(2-3):248-57. PMID:11004437<ref>PMID:11004437</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1e3t" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Rhodospirillum rubrum]] | [[Category: Rhodospirillum rubrum]] | ||
[[Category: Cotton | [[Category: Cotton NPJ]] | ||
[[Category: Jackson | [[Category: Jackson JB]] | ||
[[Category: Jeeves | [[Category: Jeeves M]] | ||
[[Category: Quirk | [[Category: Quirk PG]] | ||
[[Category: Smith | [[Category: Smith KJ]] | ||
Latest revision as of 08:29, 15 May 2024
Solution Structure of the NADP(H) binding Component (dIII) of Proton-Translocating Transhydrogenase from Rhodospirillum rubrumSolution Structure of the NADP(H) binding Component (dIII) of Proton-Translocating Transhydrogenase from Rhodospirillum rubrum
Structural highlights
FunctionPNTB_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 PubMedTranshydrogenase 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. Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum.,Jeeves M, Smith KJ, Quirk PG, Cotton NP, Jackson JB Biochim Biophys Acta. 2000 Aug 15;1459(2-3):248-57. PMID:11004437[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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