1hzz: Difference between revisions

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New page: left|200px<br /><applet load="1hzz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hzz, resolution 2.50Å" /> '''THE ASYMMETRIC COMPL...
 
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[[Image:1hzz.gif|left|200px]]<br /><applet load="1hzz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hzz, resolution 2.50&Aring;" />
'''THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE'''<br />


==Overview==
==THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE==
BACKGROUND: Membrane-bound ion translocators have important functions in, biology, but their mechanisms of action are often poorly understood., Transhydrogenase, found in animal mitochondria and bacteria, links the, redox reaction between NAD(H) and NADP(H) to proton translocation across a, membrane. Linkage is achieved through changes in protein conformation at, the nucleotide binding sites. The redox reaction takes place between two, protein components located on the membrane surface: dI, which binds, NAD(H), and dIII, which binds NADP(H). A third component, dII, provides a, proton channel through the membrane. Intact membrane-located, transhydrogenase is probably a dimer (two copies each of dI, dII, and, dIII). RESULTS: We have solved the high-resolution crystal structure of a, dI:dIII complex of transhydrogenase from Rhodospirillum rubrum-the first, from a transhydrogenase of any species. It is a heterotrimer, having two, polypeptides of dI and one of dIII. The dI polypeptides fold into a dimer., The loop on dIII, which binds the nicotinamide ring of NADP(H), is, inserted into the NAD(H) binding cleft of one of the dI polypeptides. The, cleft of the other dI is not occupied by a corresponding dIII component., CONCLUSIONS: The redox step in the transhydrogenase reaction is readily, visualized; the NC4 atoms of the nicotinamide rings of the bound, nucleotides are brought together to facilitate direct hydride transfer, with A-B stereochemistry. The asymmetry of the dI:dIII complex suggests, that in the intact enzyme there is an alternation of conformation at the, catalytic sites associated with changes in nucleotide binding during, proton translocation.
<StructureSection load='1hzz' size='340' side='right'caption='[[1hzz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hzz]] is a 3 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=1HZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <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=1hzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzz OCA], [https://pdbe.org/1hzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzz RCSB], [https://www.ebi.ac.uk/pdbsum/1hzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzz 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/hz/1hzz_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=1hzz ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HZZ 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 NAD and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HZZ OCA].
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase., Cotton NP, White SA, Peake SJ, McSweeney S, Jackson JB, Structure. 2001 Feb 7;9(2):165-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11250201 11250201]
[[Category: Large Structures]]
[[Category: NAD(P)(+) transhydrogenase (B-specific)]]
[[Category: Protein complex]]
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
[[Category: Cotton, N.P.J.]]
[[Category: Cotton NPJ]]
[[Category: Jackson, J.B.]]
[[Category: Jackson JB]]
[[Category: McSweeney, S.]]
[[Category: McSweeney S]]
[[Category: Peake, S.J.]]
[[Category: Peake SJ]]
[[Category: White, S.A.]]
[[Category: White SA]]
[[Category: NAD]]
[[Category: NAP]]
[[Category: alpha beta repeat]]
[[Category: nucleotide-binding fold]]
[[Category: rossmann fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:56:39 2007''

Latest revision as of 10:31, 7 February 2024

THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASETHE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE

Structural highlights

1hzz is a 3 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 2.5Å
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

1hzz, resolution 2.50Å

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