4o9u: Difference between revisions

Revision as of 07:13, 25 January 2023

Mechanism of transhydrogenase coupling proton translocation and hydride transfer

Structural highlights

4o9u is a 6 chain structure with sequence from Thermus thermophilus HB27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	NAD, NAP
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q72GR9_THET2

Publication Abstract from PubMed

NADPH/NADP(+) (the reduced form of NADP(+)/nicotinamide adenine dinucleotide phosphate) homeostasis is critical for countering oxidative stress in cells. Nicotinamide nucleotide transhydrogenase (TH), a membrane enzyme present in both bacteria and mitochondria, couples the proton motive force to the generation of NADPH. We present the 2.8 A crystal structure of the transmembrane proton channel domain of TH from Thermus thermophilus and the 6.9 A crystal structure of the entire enzyme (holo-TH). The membrane domain crystallized as a symmetric dimer, with each protomer containing a putative proton channel. The holo-TH is a highly asymmetric dimer with the NADP(H)-binding domain (dIII) in two different orientations. This unusual arrangement suggests a catalytic mechanism in which the two copies of dIII alternatively function in proton translocation and hydride transfer.

Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer.,Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD Science. 2015 Jan 9;347(6218):178-81. doi: 10.1126/science.1260451. PMID:25574024^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD. Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer. Science. 2015 Jan 9;347(6218):178-81. doi: 10.1126/science.1260451. PMID:25574024 doi:https://dx.doi.org/10.1126/science.1260451

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OCA

[1] Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD. Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer. Science. 2015 Jan 9;347(6218):178-81. doi: 10.1126/science.1260451. PMID:25574024 doi:https://dx.doi.org/10.1126/science.1260451

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='4o9u' size='340' side='right'caption='[[4o9u]], [[Resolution|resolution]] 6.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4o9u]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4o9u]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='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">TT_C1779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2]), TT_C1778 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2]), TT_C1780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=4o9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9u OCA], [https://pdbe.org/4o9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9u RCSB], [https://www.ebi.ac.uk/pdbsum/4o9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9u ProSAT]</span></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='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=4o9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9u OCA], [http://pdbe.org/4o9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o9u RCSB], [http://www.ebi.ac.uk/pdbsum/4o9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9u ProSAT]</span></td></tr>
 </table>
 == 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 ==
@@ Line 22: / Line 20: @@
 ==See Also==
-*[[NAD(P) transhydrogenase|NAD(P) transhydrogenase]]
+*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
 == References ==
 <references/>
@@ Line 28: / Line 26: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Thet2]]
+[[Category: Thermus thermophilus HB27]]
-[[Category: Carragher, B]]
+[[Category: Carragher B]]
-[[Category: Gennis, R B]]
+[[Category: Gennis RB]]
-[[Category: Leung, J H]]
+[[Category: Leung JH]]
-[[Category: Moeller, A]]
+[[Category: Moeller A]]
-[[Category: Potter, C S]]
+[[Category: Potter CS]]
-[[Category: Schurig-Briccio, L A]]
+[[Category: Schurig-Briccio LA]]
-[[Category: Stout, C D]]
+[[Category: Stout CD]]
-[[Category: Yamaguchi, M]]
+[[Category: Yamaguchi M]]
-[[Category: Alpha2]]
-[[Category: And domain iii as a dimer]]
-[[Category: Couples proton motive]]
-[[Category: Holo-transhydrogease from thermus thermophilus assembled from subunits alpha1]]
-[[Category: Hydride transfer]]
-[[Category: Membrane protein]]
-[[Category: Nicotinamide nucleotide transhydrogenase]]
-[[Category: Periplasmic membrane and cytosol]]
-[[Category: Proton translocation and hydride transfer]]
-[[Category: Truncated beta]]

4o9u: Difference between revisions

Revision as of 07:13, 25 January 2023

Mechanism of transhydrogenase coupling proton translocation and hydride transfer

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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