4lrs: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:


==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==
==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]] 1.55&Aring;' scene=''>
<StructureSection load='4lrs' size='340' side='right'caption='[[4lrs]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lrs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19995 Atcc 19995] and [http://en.wikipedia.org/wiki/Thecd Thecd]. 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>
<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='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>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lrt|4lrt]]</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>
<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 THECD]), Tcur_0535 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471852 THECD])</td></tr>
<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>
<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://pdbe.org/4lrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lrs RCSB], [http://www.ebi.ac.uk/pdbsum/4lrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lrs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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]  
[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==
==See Also==
*[[Aldolase|Aldolase]]
*[[Aldolase 3D structures|Aldolase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 4-hydroxy-2-oxovalerate aldolase]]
[[Category: Large Structures]]
[[Category: Atcc 19995]]
[[Category: Thermomonospora curvata]]
[[Category: Thecd]]
[[Category: Thermomonospora curvata DSM 43183]]
[[Category: Branlant, G]]
[[Category: Branlant G]]
[[Category: Fischer, B]]
[[Category: Fischer B]]
[[Category: Gruez, A]]
[[Category: Gruez A]]
[[Category: Talfournier, F]]
[[Category: Talfournier F]]
[[Category: Aldolase]]
[[Category: Dehydrogenase]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]
[[Category: Tim barrel domain]]

Revision as of 14:23, 14 December 2022

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 siteCrystal 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

Structural highlights

4lrs is a 3 chain structure with sequence from Thermomonospora curvata and Thermomonospora curvata DSM 43183. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

4lrs, resolution 1.55Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4lrs&oldid=3683708"