4lrs

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{{STRUCTURE_4lrs| PDB=4lrs | SCENE= }}
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==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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===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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<StructureSection load='4lrs' size='340' side='right' caption='[[4lrs]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4lrs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermomonospora_curvata Thermomonospora curvata] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LRS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lrt|4lrt]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tcur_0536 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471852 Thermomonospora curvata DSM 43183]), Tcur_0535 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471852 Thermomonospora curvata DSM 43183])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-2-oxovalerate_aldolase 4-hydroxy-2-oxovalerate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.39 4.1.3.39] </span></td></tr>
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<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=4lrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lrs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lrs RCSB], [http://www.ebi.ac.uk/pdbsum/4lrs PDBsum]</span></td></tr>
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</table>
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==Function==
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==See Also==
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[[http://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] [[http://www.uniprot.org/uniprot/D1A3K7_THECD D1A3K7_THECD]] Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01657]
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*[[Aldolase|Aldolase]]
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__TOC__
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==About this Structure==
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</StructureSection>
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[[4lrs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermomonospora_curvata Thermomonospora curvata] and [http://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].
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[[Category: 4-hydroxy-2-oxovalerate aldolase]]
[[Category: 4-hydroxy-2-oxovalerate aldolase]]
[[Category: Thermomonospora curvata]]
[[Category: Thermomonospora curvata]]
[[Category: Thermomonospora curvata dsm 43183]]
[[Category: Thermomonospora curvata dsm 43183]]
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[[Category: Branlant, G.]]
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[[Category: Branlant, G]]
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[[Category: Fischer, B.]]
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[[Category: Fischer, B]]
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[[Category: Gruez, A.]]
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[[Category: Gruez, A]]
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[[Category: Talfournier, F.]]
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[[Category: Talfournier, F]]
[[Category: Aldolase]]
[[Category: Aldolase]]
[[Category: Dehydrogenase]]
[[Category: Dehydrogenase]]

Revision as of 15:01, 21 December 2014

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

4lrs, resolution 1.55Å

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