4lrs: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4lrs|  PDB=4lrs  |  SCENE=  }}
===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===


The entry 4lrs is ON HOLD
==Function==
[[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]


Authors: Fischer, B., Branlant, G., Talfournier, F., Gruez, A.
==About this Structure==
 
[[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].  
Description: 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
[[Category: 4-hydroxy-2-oxovalerate aldolase]]
[[Category: Thermomonospora curvata]]
[[Category: Thermomonospora curvata dsm 43183]]
[[Category: Branlant, G.]]
[[Category: Fischer, B.]]
[[Category: Gruez, A.]]
[[Category: Talfournier, F.]]
[[Category: Aldolase]]
[[Category: Dehydrogenase]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]
[[Category: Tim barrel domain]]