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[[Image:1xlt.gif|left|200px]]


{{Structure
==Crystal structure of Transhydrogenase [(domain I)2:domain III] heterotrimer complex==
|PDB= 1xlt |SIZE=350|CAPTION= <scene name='initialview01'>1xlt</scene>, resolution 3.10&Aring;
<StructureSection load='1xlt' size='340' side='right'caption='[[1xlt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene>
<table><tr><td colspan='2'>[[1xlt]] is a 9 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=1XLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLT FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
|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])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=1xlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlt OCA], [https://pdbe.org/1xlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xlt RCSB], [https://www.ebi.ac.uk/pdbsum/1xlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xlt ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
[[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/xl/1xlt_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=1xlt ConSurf].
<div style="clear:both"></div>


'''Crystal structure of Transhydrogenase [(domain I)2:domain III] heterotrimer complex'''
==See Also==
 
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Transhydrogenase (TH) couples direct and stereospecific hydride transfer between NAD(H) and NADP(H), bound within soluble domains I and III, respectively, to proton translocation across membrane bound domain II. The cocrystal structure of Rhodospirillum rubrum TH domains I and III has been determined in the presence of limiting NADH, under conditions in which the subunits reach equilibrium during crystallization. The crystals contain three heterotrimeric complexes, dI(2)dIII, in the asymmetric unit. Multiple conformations of loops and side-chains, and NAD(H) cofactors, are observed in domain I pertaining to substrate/product exchange, and highlighting electrostatic interactions during the hydride transfer. Two interacting NAD(H)-NADPH pairs are observed where alternate conformations of the NAD(H) phosphodiester and conserved arginine side-chains are correlated. In addition, the stereochemistry of one NAD(H)-NADPH pair approaches that expected for nicotinamide hydride transfer reactions. The cocrystal structure exhibits non-crystallographic symmetry that implies another orientation for domain III, which could occur in dimeric TH. Superposition of the "closed" form of domain III (PDB 1PNO, chain A) onto the dI(2)dIII complex reveals a severe steric conflict of highly conserved loops in domains I and III. This overlap, and the overlap with a 2-fold related domain III, suggests that motions of loop D within domain III and of the entire domain are correlated during turnover. The results support the concept that proton pumping in TH is driven by the difference in binding affinity for oxidized and reduced nicotinamide cofactors, and in the absence of a difference in redox potential, must occur through conformational effects.
[[Category: Large Structures]]
 
==About this Structure==
1XLT 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=1XLT OCA].
 
==Reference==
Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains., Sundaresan V, Chartron J, Yamaguchi M, Stout CD, J Mol Biol. 2005 Feb 18;346(2):617-29. Epub 2004 Dec 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15670609 15670609]
[[Category: NAD(P)(+) transhydrogenase (AB-specific)]]
[[Category: Protein complex]]
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
[[Category: Chartron, J.]]
[[Category: Chartron J]]
[[Category: Stout, C D.]]
[[Category: Stout CD]]
[[Category: Sundaresan, V.]]
[[Category: Sundaresan V]]
[[Category: Yamaguchi, M.]]
[[Category: Yamaguchi M]]
[[Category: NA]]
[[Category: NAD]]
[[Category: NDP]]
[[Category: SUC]]
[[Category: nad]]
[[Category: nadh]]
[[Category: nadp]]
[[Category: nadph]]
[[Category: transhydrogenase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:11:34 2008''

Latest revision as of 11:51, 14 February 2024

Crystal structure of Transhydrogenase [(domain I)2:domain III] heterotrimer complexCrystal structure of Transhydrogenase [(domain I)2:domain III] heterotrimer complex

Structural highlights

1xlt is a 9 chain structure with sequence from Rhodospirillum rubrum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.1Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1xlt, resolution 3.10Å

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