1hzz: Difference between revisions

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<StructureSection load='1hzz' size='340' side='right'caption='[[1hzz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1hzz' size='340' side='right'caption='[[1hzz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hzz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"dicrospirillum_rubrum"_enderlein_1925 "dicrospirillum rubrum" enderlein 1925]. 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>
<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='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>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1djl|1djl]], [[1e3t|1e3t]], [[1f8g|1f8g]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PNTAA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 "Dicrospirillum rubrum" Enderlein 1925]), PNTB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 "Dicrospirillum rubrum" Enderlein 1925])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(B-specific) NAD(P)(+) transhydrogenase (B-specific)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.1 1.6.1.1] </span></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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PNTAA_RHORU PNTAA_RHORU]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity). [[https://www.uniprot.org/uniprot/PNTB_RHORU PNTB_RHORU]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1hzz ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:11250201<ref>PMID:11250201</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hzz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dicrospirillum rubrum enderlein 1925]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cotton, N P.J]]
[[Category: Rhodospirillum rubrum]]
[[Category: Jackson, J B]]
[[Category: Cotton NPJ]]
[[Category: McSweeney, S]]
[[Category: Jackson JB]]
[[Category: Peake, S J]]
[[Category: McSweeney S]]
[[Category: White, S A]]
[[Category: Peake SJ]]
[[Category: Alpha beta repeat]]
[[Category: White SA]]
[[Category: Nucleotide-binding fold]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]

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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