4o9p

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(Difference between revisions)

Revision as of 09:49, 11 August 2016

Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer SeMet derivative

Structural highlights

4o9p is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Activity:	NAD(P)(+) transhydrogenase (Re/Si-specific), with EC number 1.6.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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]

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:http://dx.doi.org/10.1126/science.1260451

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4o9p"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer SeMet derivative==
 <StructureSection load='4o9p' size='340' side='right' caption='[[4o9p]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4o9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o9p RCSB], [http://www.ebi.ac.uk/pdbsum/4o9p PDBsum]</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=4o9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9p OCA], [http://pdbe.org/4o9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o9p RCSB], [http://www.ebi.ac.uk/pdbsum/4o9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9p ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4o9p" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[NAD(P) transhydrogenase|NAD(P) transhydrogenase]]
 == References ==
 <references/>

4o9p

From Proteopedia

Revision as of 09:49, 11 August 2016

Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer SeMet derivative

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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