1u2g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:37, 23 August 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1u2g.png|left|200px]]
 
-
<!--
+
==transhydrogenase (dI.ADPr)2(dIII.NADPH)1 asymmetric complex==
-
The line below this paragraph, containing "STRUCTURE_1u2g", creates the "Structure Box" on the page.
+
<StructureSection load='1u2g' size='340' side='right'caption='[[1u2g]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1u2g]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2G FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-
{{STRUCTURE_1u2g| PDB=1u2g | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2g OCA], [https://pdbe.org/1u2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2g RCSB], [https://www.ebi.ac.uk/pdbsum/1u2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2g ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PNTAA_RHORT PNTAA_RHORT] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.[UniProtKB:P07001]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u2g_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u2g ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===transhydrogenase (dI.ADPr)2(dIII.NADPH)1 asymmetric complex===
+
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<ref>PMID:15323555</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1u2g" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_15323555}}, adds the Publication Abstract to the page
+
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 15323555 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15323555}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1U2G is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2G OCA].
+
-
 
+
-
==Reference==
+
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/15323555 15323555]
+
-
[[Category: Protein complex]]
+
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
-
[[Category: Boxel, G I.van.]]
+
[[Category: Jackson JB]]
-
[[Category: Jackson, J B.]]
+
[[Category: Mather OC]]
-
[[Category: Mather, O C.]]
+
[[Category: Singh A]]
-
[[Category: Singh, A.]]
+
[[Category: White SA]]
-
[[Category: White, S A.]]
+
[[Category: Van Boxel GI]]
-
[[Category: Nad+]]
+
-
[[Category: Nadp+]]
+
-
[[Category: Oxidoreductase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:03:48 2008''
+

Current revision

transhydrogenase (dI.ADPr)2(dIII.NADPH)1 asymmetric complex

PDB ID 1u2g

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u2g"
Personal tools