2a87: Difference between revisions

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-[[Image:2a87.gif|left|200px]]
- {{Structure
+==Crystal Structure of M. tuberculosis Thioredoxin reductase==
-|PDB= 2a87 |SIZE=350|CAPTION= <scene name='initialview01'>2a87</scene>, resolution 3.00&Aring;
+<StructureSection load='2a87' size='340' side='right'caption='[[2a87]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
+<table><tr><td colspan='2'>[[2a87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A87 FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-|GENE= trxB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
+<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=MG:MAGNESIUM+ION'>MG</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=2a87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a87 OCA], [https://pdbe.org/2a87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a87 RCSB], [https://www.ebi.ac.uk/pdbsum/2a87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a87 ProSAT], [https://www.topsan.org/Proteins/TBSGC/2a87 TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRXB_MYCTU TRXB_MYCTU]
+== 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/a8/2a87_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=2a87 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The thioredoxin system exists ubiquitously and participates in essential antioxidant and redox-regulation processes via a pair of conserved cysteine residues. In Mycobacterium tuberculosis, which lacks a genuine glutathione system, the thioredoxin system provides reducing equivalents inside the cell. The three-dimensional structure of thioredoxin reductase from M. tuberculosis has been determined at 3 A resolution. TLS refinement reveals a large libration axis, showing that NADPH-binding domain has large anisotropic disorder. The relative rotation of the NADPH domain with respect to the FAD domain is necessary for the thioredoxin reduction cycle, as it brings the spatially distant reacting sites close together. Normal-mode analysis carried out based on the elastic network model shows that the motion required to bring about the functional conformational change can be accounted for by motion along one single mode. TLS refinement and normal-mode analysis thus enhance our understanding of the associated conformational changes.
-'''Crystal Structure of M. tuberculosis Thioredoxin reductase'''
+Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis.,Akif M, Suhre K, Verma C, Mande SC Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1603-11. Epub 2005, Nov 19. PMID:16301794<ref>PMID:16301794</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2a87" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The thioredoxin system exists ubiquitously and participates in essential antioxidant and redox-regulation processes via a pair of conserved cysteine residues. In Mycobacterium tuberculosis, which lacks a genuine glutathione system, the thioredoxin system provides reducing equivalents inside the cell. The three-dimensional structure of thioredoxin reductase from M. tuberculosis has been determined at 3 A resolution. TLS refinement reveals a large libration axis, showing that NADPH-binding domain has large anisotropic disorder. The relative rotation of the NADPH domain with respect to the FAD domain is necessary for the thioredoxin reduction cycle, as it brings the spatially distant reacting sites close together. Normal-mode analysis carried out based on the elastic network model shows that the motion required to bring about the functional conformational change can be accounted for by motion along one single mode. TLS refinement and normal-mode analysis thus enhance our understanding of the associated conformational changes.
+*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-A87 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A87 OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis., Akif M, Suhre K, Verma C, Mande SC, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1603-11. Epub 2005, Nov 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16301794 16301794]
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Single protein]]
+[[Category: Akif M]]
-[[Category: Thioredoxin-disulfide reductase]]
+[[Category: Mande SC]]
-[[Category: Akif, M.]]
+[[Category: Suhre K]]
-[[Category: Mande, S C.]]
+[[Category: Verma C]]
-[[Category: Suhre, K.]]
-[[Category: TBSGC, TB Structural Genomics Consortium.]]
-[[Category: Verma, C.]]
-[[Category: FAD]]
-[[Category: MG]]
-[[Category: NAP]]
-[[Category: fad]]
-[[Category: nap]]
-[[Category: nma]]
-[[Category: oxidoreductase]]
-[[Category: protein structure initiative]]
-[[Category: psi]]
-[[Category: structural genomic]]
-[[Category: tb structural genomics consortium]]
-[[Category: tbsgc]]
-[[Category: thioredoxin reductase]]
-[[Category: tl]]
-[[Category: trxr]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:46:31 2008''