4lrs
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4lrs is ON HOLD Authors: Fischer, B., Branlant, G., Talfournier, F., Gruez, A. Description: Crystal and solution structures of the bifunctional enz...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site== | |
| + | <StructureSection load='4lrs' size='340' side='right'caption='[[4lrs]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4lrs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata Thermomonospora curvata] and [https://en.wikipedia.org/wiki/Thermomonospora_curvata_DSM_43183 Thermomonospora curvata DSM 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LRS 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]] 1.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4lrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lrs OCA], [https://pdbe.org/4lrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lrs RCSB], [https://www.ebi.ac.uk/pdbsum/4lrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lrs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D1A3K8_THECD D1A3K8_THECD] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01656] | ||
| - | + | ==See Also== | |
| - | + | *[[Aldolase 3D structures|Aldolase 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermomonospora curvata]] | ||
| + | [[Category: Thermomonospora curvata DSM 43183]] | ||
| + | [[Category: Branlant G]] | ||
| + | [[Category: Fischer B]] | ||
| + | [[Category: Gruez A]] | ||
| + | [[Category: Talfournier F]] | ||
Current revision
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
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