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1d4o

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[[Image:1d4o.jpg|left|200px]]<br /><applet load="1d4o" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d4o, resolution 1.21&Aring;" />
 
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'''CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION==
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The nicotinamide nucleotide transhydrogenases (TH) of mitochondria and bacteria are membrane-intercalated proton pumps that transduce substrate binding energy and protonmotive force via protein conformational changes. In mitochondria, TH utilizes protonmotive force to promote direct hydride ion transfer from NADH to NADP, which are bound at the distinct extramembranous domains I and III, respectively. Domain II is the membrane-intercalated domain and contains the enzyme's proton channel. This paper describes the crystal structure of the NADP(H) binding domain III of bovine TH at 1.2 A resolution. The structure reveals that NADP is bound in a manner inverted from that previously observed for nucleotide binding folds. The non-classical binding mode exposes the NADP(H) nicotinamide ring for direct contact with NAD(H) in domain I, in accord with biochemical data. The surface of domain III surrounding the exposed nicotinamide is comprised of conserved residues presumed to form the interface with domain I during hydride ion transfer. Further, an adjacent region contains a number of acidic residues, forming a surface with negative electrostatic potential which may interact with extramembranous loops of domain II. Together, the distinctive surface features allow mechanistic considerations regarding the NADP(H)-promoted conformation changes that are involved in the interactions of domain III with domains I and II for hydride ion transfer and proton translocation.
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<StructureSection load='1d4o' size='340' side='right'caption='[[1d4o]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d4o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D4O FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.21&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4o OCA], [https://pdbe.org/1d4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d4o RCSB], [https://www.ebi.ac.uk/pdbsum/1d4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d4o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NNTM_BOVIN NNTM_BOVIN] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/1d4o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1d4o ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1D4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4O OCA].
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*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of transhydrogenase domain III at 1.2 A resolution., Prasad GS, Sridhar V, Yamaguchi M, Hatefi Y, Stout CD, Nat Struct Biol. 1999 Dec;6(12):1126-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10581554 10581554]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: NAD(P)(+) transhydrogenase (B-specific)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Hatefi Y]]
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[[Category: Hatefi, Y.]]
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[[Category: Prasad GS]]
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[[Category: Prasad, G S.]]
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[[Category: Sridhar V]]
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[[Category: Sridhar, V.]]
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[[Category: Stout CD]]
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[[Category: Stout, C D.]]
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[[Category: Yamaguchi M]]
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[[Category: Yamaguchi, M.]]
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[[Category: NAP]]
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[[Category: inverted binding of nadp(h)]]
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[[Category: nucleotide-binding fold]]
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[[Category: protein-nadp(h) complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:59 2008''
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Current revision

CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION

PDB ID 1d4o

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