1x14: Difference between revisions

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-[[Image:1x14.gif|left|200px]]
- {{Structure
+==Crystal structure of E. coli transhydrogenase domain I with bound NAD==
-|PDB= 1x14 |SIZE=350|CAPTION= <scene name='initialview01'>1x14</scene>, resolution 1.94&Aring;
+<StructureSection load='1x14' size='340' side='right'caption='[[1x14]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
+<table><tr><td colspan='2'>[[1x14]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X14 FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(AB-specific) NAD(P)(+) transhydrogenase (AB-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
-|GENE= pntA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+<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></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=1x14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x14 OCA], [https://pdbe.org/1x14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x14 RCSB], [https://www.ebi.ac.uk/pdbsum/1x14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x14 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PNTA_ECOLI PNTA_ECOLI] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
+== 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/x1/1x14_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=1x14 ConSurf].
+<div style="clear:both"></div>
-'''Crystal structure of E. coli transhydrogenase domain I with bound NAD'''
+==See Also==
+*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The dimeric integral membrane protein nicotinamide nucleotide transhydrogenase is required for cellular regeneration of NADPH in mitochondria and prokaryotes, for detoxification and biosynthesis purposes. Under physiological conditions, transhydrogenase couples the reversible reduction of NADP+ by NADH to an inward proton translocation across the membrane. Here, we present crystal structures of the NAD(H)-binding domain I of transhydrogenase from Escherichia coli, in the absence as well as in the presence of oxidized and reduced substrate. The structures were determined at 1.9-2.0 A resolution. Overall, the structures are highly similar to the crystal structure of a previously published NAD(H)-binding domain, from Rhodospirillum rubrum transhydrogenase. However, this particular domain is unique, since it is covalently connected to the integral-membrane part of transhydrogenase. Comparative studies between the structures of the two species reveal extensively differing surface properties and point to the possible importance of a rigid peptide (PAPP) in the connecting linker for conformational coupling. Further, the kinetic analysis of a deletion mutant, from which the protruding beta-hairpin was removed, indicates that this structural element is important for catalytic activity, but not for domain I:domain III interaction or dimer formation. Taken together, these results have important implications for the enzyme mechanism of the large group of transhydrogenases, including mammalian enzymes, which contain a connecting linker between domains I and II.
-==About this Structure==
-X14 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X14 OCA].
-==Reference==
-X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli., Johansson T, Oswald C, Pedersen A, Tornroth S, Okvist M, Karlsson BG, Rydstrom J, Krengel U, J Mol Biol. 2005 Sep 16;352(2):299-312. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16083909 16083909]
 [[Category: Escherichia coli]]
-[[Category: NAD(P)(+) transhydrogenase (AB-specific)]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Johansson T]]
-[[Category: Johansson, T.]]
+[[Category: Karlsson BG]]
-[[Category: Karlsson, B G.]]
+[[Category: Krengel U]]
-[[Category: Krengel, U.]]
+[[Category: Okvist M]]
-[[Category: Okvist, M.]]
+[[Category: Oswald C]]
-[[Category: Oswald, C.]]
+[[Category: Pedersen A]]
-[[Category: Pedersen, A.]]
+[[Category: Rydstrom J]]
-[[Category: Rydstrom, J.]]
+[[Category: Tornroth S]]
-[[Category: Tornroth, S.]]
-[[Category: NAD]]
-[[Category: nad(h)-binding domain]]
-[[Category: rossmann fold]]
-[[Category: transhydrogenase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:03:54 2008''