5uni: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Critical role of water molecules for proton translocation of the membrane-bound transhydrogenase==
==Critical role of water molecules for proton translocation of the membrane-bound transhydrogenase==
<StructureSection load='5uni' size='340' side='right' caption='[[5uni]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5uni' size='340' side='right'caption='[[5uni]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5uni]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UNI FirstGlance]. <br>
<table><tr><td colspan='2'>[[5uni]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UNI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.2&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5uni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uni OCA], [http://pdbe.org/5uni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uni RCSB], [http://www.ebi.ac.uk/pdbsum/5uni PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uni 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=5uni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uni OCA], [https://pdbe.org/5uni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uni RCSB], [https://www.ebi.ac.uk/pdbsum/5uni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uni ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q72GS0_THET2 Q72GS0_THET2]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).[PIRNR:PIRNR000204]
[https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nicotinamide nucleotide transhydrogenase (TH) is an integral membrane enzyme that uses the proton-motive force to drive hydride transfer from NADH to NADP+ in bacteria and eukaryotes. Here we solved a 2.2-A crystal structure of the TH transmembrane domain (Thermus thermophilus) at pH 6.5. This structure exhibits conformational changes of helix positions from a previous structure solved at pH 8.5, and reveals internal water molecules interacting with residues implicated in proton translocation. Together with molecular dynamics simulations, we show that transient water flows across a narrow pore and a hydrophobic "dry" region in the middle of the membrane channel, with key residues His42alpha2 (chain A) being protonated and Thr214beta (chain B) displaying a conformational change, respectively, to gate the channel access to both cytoplasmic and periplasmic chambers. Mutation of Thr214beta to Ala deactivated the enzyme. These data provide new insights into the gating mechanism of proton translocation in TH.


Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase.,Padayatti PS, Leung JH, Mahinthichaichan P, Tajkhorshid E, Ishchenko A, Cherezov V, Soltis SM, Jackson JB, Stout CD, Gennis RB, Zhang Q Structure. 2017 Jul 5;25(7):1111-1119.e3. doi: 10.1016/j.str.2017.05.022. Epub, 2017 Jun 22. PMID:28648609<ref>PMID:28648609</ref>
==See Also==
 
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5uni" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Leung, J H]]
[[Category: Large Structures]]
[[Category: Padayatti, P S]]
[[Category: Thermus thermophilus]]
[[Category: High resolution]]
[[Category: Leung JH]]
[[Category: Oxidoreductase]]
[[Category: Padayatti PS]]
[[Category: Proton channel]]
[[Category: Transmembrane]]

Latest revision as of 17:28, 6 March 2024

Critical role of water molecules for proton translocation of the membrane-bound transhydrogenaseCritical role of water molecules for proton translocation of the membrane-bound transhydrogenase

Structural highlights

5uni is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q72GR9_THET2

See Also

5uni, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=5uni&oldid=4082783"