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| | <StructureSection load='5wed' size='340' side='right'caption='[[5wed]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='5wed' size='340' side='right'caption='[[5wed]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wed]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Caltt Caltt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WED FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wed]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldalkalibacillus_thermarum_TA2.A1 Caldalkalibacillus thermarum TA2.A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WED FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nwz|4nwz]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CathTA2_0279 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=986075 CALTT])</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=5wed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wed OCA], [https://pdbe.org/5wed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wed RCSB], [https://www.ebi.ac.uk/pdbsum/5wed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wed ProSAT]</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=5wed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wed OCA], [http://pdbe.org/5wed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wed RCSB], [http://www.ebi.ac.uk/pdbsum/5wed PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wed ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F5L3B8_CALTT F5L3B8_CALTT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caltt]] | + | [[Category: Caldalkalibacillus thermarum TA2 A1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aragao, D]] | + | [[Category: Aragao D]] |
| - | [[Category: Cook, G M]] | + | [[Category: Cook GM]] |
| - | [[Category: Nakatani, Y]] | + | [[Category: Nakatani Y]] |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Membrane/cytoplasm]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
F5L3B8_CALTT
Publication Abstract from PubMed
Type II NADH:quinone oxidoreductase (NDH-2) is a respiratory enzyme found in the electron-transport chain of many species, with the exception of mammals. It is a 40-70 kDa single-subunit monotopic membrane protein that catalyses the oxidation of NADH and the reduction of quinone molecules via the cofactor FAD. NDH-2 is a promising new target for drug development given its essential role in many bacterial species and intracellular parasites. Only two bacterial NDH-2 structures have been reported and these structures are at moderate resolution (2.3-2.5 A). In this communication, a new crystallization platform is reported that produced high-quality NDH-2 crystals that diffracted to high resolution (2.15 A). The high-resolution NDH-2 structure was used for in silico quinone substrate-docking studies to investigate the binding poses of menadione and ubiquinone molecules. These studies revealed that a very limited number of molecular interactions occur at the quinone-binding site of NDH-2. Given that the conformation of the active site is well defined, this high-resolution structure is potentially suitable for in silico inhibitor-compound screening and ligand-docking applications.
Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 A.,Nakatani Y, Jiao W, Aragao D, Shimaki Y, Petri J, Parker EJ, Cook GM Acta Crystallogr F Struct Biol Commun. 2017 Oct 1;73(Pt 10):541-549. doi:, 10.1107/S2053230X17013073. Epub 2017 Sep 23. PMID:28994401[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakatani Y, Jiao W, Aragao D, Shimaki Y, Petri J, Parker EJ, Cook GM. Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 A. Acta Crystallogr F Struct Biol Commun. 2017 Oct 1;73(Pt 10):541-549. doi:, 10.1107/S2053230X17013073. Epub 2017 Sep 23. PMID:28994401 doi:http://dx.doi.org/10.1107/S2053230X17013073
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