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1u28

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Revision as of 08:53, 21 March 2018

R. rubrum transhydrogenase asymmetric complex (dI.NAD+)2(dIII.NADP+)1

Structural highlights

1u28 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:	1hzz, 1nm5, 1ptj, 1u2d, 1u2g, 1u31
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 (hydride-transfer) reaction between NAD(H) and NADP(H) to proton translocation across a membrane. The redox reaction is catalyzed at the interface between two components (dI and dIII) which protrude from the membrane. A complex formed from recombinant dI and dIII (the dI(2)dIII(1) complex) from Rhodospirillum rubrum transhydrogenase catalyzes fast single-turnover hydride transfer between bound nucleotides. In this report we describe three new crystal structures of the dI(2)dIII(1) complex in different nucleotide-bound forms. The structures reveal an asymmetry in nucleotide binding that complements results from solution studies and supports the notion that intact transhydrogenase functions by an alternating site mechanism. In one structure, the redox site is occupied by NADH (on dI) and NADPH (on dIII). The dihydronicotinamide rings take up positions which may approximate to the ground state for hydride transfer: the redox-active C4(N) atoms are separated by only 3.6 A, and the perceived reaction stereochemistry matches that observed experimentally. The NADH conformation is different in the two dI polypeptides of this form of the dI(2)dIII(1) complex. Comparisons between a number of X-ray structures show that a conformational change in the NADH is driven by relative movement of the two domains which comprise dI. It is suggested that an equivalent conformational change in the intact enzyme is important in gating the hydride-transfer reaction. The observed nucleotide conformational change in the dI(2)dIII(1) complex is accompanied by rearrangements in the orientation of local amino acid side chains which may be responsible for sealing the site from the solvent and polarizing hydride transfer.

Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase.,Mather OC, Singh A, van Boxel GI, White SA, Jackson JB Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:15323555^[1]

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

References

↑ Mather OC, Singh A, van Boxel GI, White SA, Jackson JB. Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:15323555 doi:10.1021/bi0497594

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u28"

@@ Line 1: / Line 1: @@
 ==R. rubrum transhydrogenase asymmetric complex (dI.NAD+)2(dIII.NADP+)1==
 <StructureSection load='1u28' size='340' side='right' caption='[[1u28]], [[Resolution|resolution]] 2.30&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=1u28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u28 OCA], [http://pdbe.org/1u28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u28 RCSB], [http://www.ebi.ac.uk/pdbsum/1u28 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=1u28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u28 OCA], [http://pdbe.org/1u28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u28 RCSB], [http://www.ebi.ac.uk/pdbsum/1u28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u28 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/u2/1u28_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u28_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1u28

From Proteopedia

Revision as of 08:53, 21 March 2018

R. rubrum transhydrogenase asymmetric complex (dI.NAD+)2(dIII.NADP+)1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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