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2oor

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Revision as of 18:56, 24 January 2018

Structure of transhydrogenase (dI.NAD+)2(dIII.H2NADPH)1 asymmetric complex

Structural highlights

2oor is a 3 chain structure with sequence from "dicrospirillum_rubrum"_enderlein_1925 "dicrospirillum rubrum" enderlein 1925. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1u2d, 1hzz, 2oo5
Gene:	pntAA, nntA1 ("Dicrospirillum rubrum" Enderlein 1925), pntB, nntB ("Dicrospirillum rubrum" Enderlein 1925)
Activity:	NAD(P)(+) transhydrogenase (Re/Si-specific), with EC number 1.6.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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). [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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Transhydrogenase couples the redox reaction between NADH and NADP+ to proton translocation across a membrane. The enzyme comprises three components; dI binds NAD(H), dIII binds NADP(H), and dII spans the membrane. The 1,4,5,6-tetrahydro analogue of NADH (designated H2NADH) bound to isolated dI from Rhodospirillum rubrum transhydrogenase with similar affinity to the physiological nucleotide. Binding of either NADH or H2NADH led to closure of the dI mobile loop. The 1,4,5,6-tetrahydro analogue of NADPH (H2NADPH) bound very tightly to isolated R. rubrum dIII, but the rate constant for dissociation was greater than that for NADPH. The replacement of NADP+ on dIII either with H2NADPH or with NADPH caused a similar set of chemical shift alterations, signifying an equivalent conformational change. Despite similar binding properties to the natural nucleotides, neither H2NADH nor H2NADPH could serve as a hydride donor in transhydrogenation reactions. Mixtures of dI and dIII form dI2dIII1 complexes. The nucleotide charge distribution of complexes loaded either with H2NADH and NADP+ or with NAD+ and H2NADPH should more closely mimic the ground states for forward and reverse hydride transfer, respectively, than previously studied dead-end species. Crystal structures of such complexes at 2.6 and 2.3 A resolution are described. A transition state for hydride transfer between dihydronicotinamide and nicotinamide derivatives determined in ab initio quantum mechanical calculations resembles the organization of nucleotides in the transhydrogenase active site in the crystal structure. Molecular dynamics simulations of the enzyme indicate that the (dihydro)nicotinamide rings remain close to a ground state for hydride transfer throughout a 1.4 ns trajectory.

Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries.,Bhakta T, Whitehead SJ, Snaith JS, Dafforn TR, Wilkie J, Rajesh S, White SA, Jackson JB Biochemistry. 2007 Mar 20;46(11):3304-18. Epub 2007 Feb 27. PMID:17323922^[1]

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

References

↑ Bhakta T, Whitehead SJ, Snaith JS, Dafforn TR, Wilkie J, Rajesh S, White SA, Jackson JB. Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries. Biochemistry. 2007 Mar 20;46(11):3304-18. Epub 2007 Feb 27. PMID:17323922 doi:10.1021/bi061843r

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2oor"

Categories: Dicrospirillum rubrum enderlein 1925 | Bhakta, T | Jackson, J B | Oxidoreductase | Rossmann fold

@@ Line 1: / Line 1: @@
 ==Structure of transhydrogenase (dI.NAD+)2(dIII.H2NADPH)1 asymmetric complex==
 <StructureSection load='2oor' size='340' side='right' caption='[[2oor]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pntAA, nntA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 "Dicrospirillum rubrum" Enderlein 1925]), pntB, nntB ([http://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'>[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=2oor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oor OCA], [http://pdbe.org/2oor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oor RCSB], [http://www.ebi.ac.uk/pdbsum/2oor 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=2oor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oor OCA], [http://pdbe.org/2oor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oor RCSB], [http://www.ebi.ac.uk/pdbsum/2oor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oor ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oo/2oor_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oo/2oor_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 2oor" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[NAD(P) transhydrogenase|NAD(P) transhydrogenase]]
 == References ==
 <references/>
@@ Line 39: / Line 37: @@
 [[Category: Dicrospirillum rubrum enderlein 1925]]
 [[Category: Bhakta, T]]
-[[Category: J B., Jackson]]
+[[Category: Jackson, J B]]
 [[Category: Oxidoreductase]]
 [[Category: Rossmann fold]]

2oor

From Proteopedia

Revision as of 18:56, 24 January 2018

Structure of transhydrogenase (dI.NAD+)2(dIII.H2NADPH)1 asymmetric complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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