2q0l: Difference between revisions
No edit summary |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Helicobacter pylori thioredoxin reductase reduced by sodium dithionite in complex with NADP+== | ||
<StructureSection load='2q0l' size='340' side='right'caption='[[2q0l]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2q0l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q0L FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=2q0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0l OCA], [https://pdbe.org/2q0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q0l RCSB], [https://www.ebi.ac.uk/pdbsum/2q0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q0l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRXB_HELPY TRXB_HELPY] | |||
== 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/q0/2q0l_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2q0l ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structures of homodimeric thioredoxin reductase (TrxR) from the gastric pathogen Helicobacter pylori in complex with NADP(+) have been determined for the oxidized and reduced form of the enzyme at 1.7 and 1.45 A resolution, respectively. The enzyme subunit is built up of FAD- and NAD(P)H-binding domains, each of which contain variants of the Rossmann fold typical of nucleotide-binding proteins. The majority of the amino-acid residues binding the cofactors FAD and NAD(P)H are conserved in the low-molecular-weight thioredoxin reductases. In the reduced species the isoalloxazine ring of FAD is bent along an axis passing through the N5 and N10 atoms with an angle of 22 degrees and the ribityl moiety adopts an unusual conformation. Well defined electron density shows the position of the whole NADP(+) molecule with a binding mode similar to that observed in the Escherichia coli TrxR-thioredoxin complex, although the orientation of the NAD(P)H-binding domain is different. Rigid-body rotation of this domain to the orientation observed in the E. coli TrxR-thioredoxin complex positions NADP(+) adjacent to the FAD molecule, suitable for electron transfer, without any readjustments of the conformation of NADP(+). A comparison of the binding surfaces of thioredoxin and thioredoxin reductases from H. pylori and E. coli shows that the overall surface charge distribution in these proteins is conserved and that residue substitutions that change the shape of the binding surface may account for the species-specific recognition of thioredoxin by TrxR. | |||
High-resolution structures of oxidized and reduced thioredoxin reductase from Helicobacter pylori.,Gustafsson TN, Sandalova T, Lu J, Holmgren A, Schneider G Acta Crystallogr D Biol Crystallogr. 2007 Jul;63(Pt 7):833-43. Epub 2007, Jun 15. PMID:17582174<ref>PMID:17582174</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2q0l" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Helicobacter pylori 26695]] | ||
[[Category: Large Structures]] | |||
[[Category: Gustafsson T]] | |||
== | [[Category: Holmgren A]] | ||
[[Category: Lu J]] | |||
[[Category: Helicobacter pylori]] | [[Category: Sandalova T]] | ||
[[Category: | [[Category: Schneider G]] | ||
[[Category: Gustafsson | |||
[[Category: Holmgren | |||
[[Category: Lu | |||
[[Category: Sandalova | |||
[[Category: Schneider | |||
Latest revision as of 11:31, 30 October 2024
Helicobacter pylori thioredoxin reductase reduced by sodium dithionite in complex with NADP+Helicobacter pylori thioredoxin reductase reduced by sodium dithionite in complex with NADP+
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structures of homodimeric thioredoxin reductase (TrxR) from the gastric pathogen Helicobacter pylori in complex with NADP(+) have been determined for the oxidized and reduced form of the enzyme at 1.7 and 1.45 A resolution, respectively. The enzyme subunit is built up of FAD- and NAD(P)H-binding domains, each of which contain variants of the Rossmann fold typical of nucleotide-binding proteins. The majority of the amino-acid residues binding the cofactors FAD and NAD(P)H are conserved in the low-molecular-weight thioredoxin reductases. In the reduced species the isoalloxazine ring of FAD is bent along an axis passing through the N5 and N10 atoms with an angle of 22 degrees and the ribityl moiety adopts an unusual conformation. Well defined electron density shows the position of the whole NADP(+) molecule with a binding mode similar to that observed in the Escherichia coli TrxR-thioredoxin complex, although the orientation of the NAD(P)H-binding domain is different. Rigid-body rotation of this domain to the orientation observed in the E. coli TrxR-thioredoxin complex positions NADP(+) adjacent to the FAD molecule, suitable for electron transfer, without any readjustments of the conformation of NADP(+). A comparison of the binding surfaces of thioredoxin and thioredoxin reductases from H. pylori and E. coli shows that the overall surface charge distribution in these proteins is conserved and that residue substitutions that change the shape of the binding surface may account for the species-specific recognition of thioredoxin by TrxR. High-resolution structures of oxidized and reduced thioredoxin reductase from Helicobacter pylori.,Gustafsson TN, Sandalova T, Lu J, Holmgren A, Schneider G Acta Crystallogr D Biol Crystallogr. 2007 Jul;63(Pt 7):833-43. Epub 2007, Jun 15. PMID:17582174[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||