6ok1: Difference between revisions

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<StructureSection load='6ok1' size='340' side='right'caption='[[6ok1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6ok1' size='340' side='right'caption='[[6ok1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ok1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OK1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ok1]] is a 4 chain structure with sequence from [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=6OK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OK1 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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7&#8491;</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=6ok1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ok1 OCA], [http://pdbe.org/6ok1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ok1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ok1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ok1 ProSAT]</span></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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6ok1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ok1 OCA], [https://pdbe.org/6ok1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ok1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ok1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ok1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LTP2_THECD LTP2_THECD] Probably involved in bile acid degradation (Probable). In vitro, when associated with the ChsH1/ChsH2 hydratase, catalyzes the retroaldol cleavage of 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA (17-HOPC-CoA), forming androst-4-ene-3,17-dione and propionyl-CoA (PubMed:31209106). The in vivo substrate is probably a closely analogous bile acid degradation metabolite (Probable).<ref>PMID:31209106</ref> <ref>PMID:31209106</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aggett, R]]
[[Category: Thermomonospora curvata DSM 43183]]
[[Category: Kimber, M S]]
[[Category: Aggett R]]
[[Category: Mallette, E]]
[[Category: Kimber MS]]
[[Category: Seah, S Y.K]]
[[Category: Mallette E]]
[[Category: Aldolase]]
[[Category: Seah SYK]]
[[Category: Cholesterol degradation]]
[[Category: Duf35 domain]]
[[Category: Thiolase superfamily]]
[[Category: Transport protein]]

Latest revision as of 17:52, 13 March 2024

Ltp2-ChsH2(DUF35) aldolaseLtp2-ChsH2(DUF35) aldolase

Structural highlights

6ok1 is a 4 chain structure with sequence from Thermomonospora curvata DSM 43183. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LTP2_THECD Probably involved in bile acid degradation (Probable). In vitro, when associated with the ChsH1/ChsH2 hydratase, catalyzes the retroaldol cleavage of 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA (17-HOPC-CoA), forming androst-4-ene-3,17-dione and propionyl-CoA (PubMed:31209106). The in vivo substrate is probably a closely analogous bile acid degradation metabolite (Probable).[1] [2]

References

  1. ↑ Aggett R, Mallette E, Gilbert SE, Vachon MA, Schroeter KL, Kimber MS, Seah SYK. The steroid side chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site. J Biol Chem. 2019 Jun 16. pii: RA119.008889. doi: 10.1074/jbc.RA119.008889. PMID:31209106 doi:http://dx.doi.org/10.1074/jbc.RA119.008889
  2. ↑ Aggett R, Mallette E, Gilbert SE, Vachon MA, Schroeter KL, Kimber MS, Seah SYK. The steroid side chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site. J Biol Chem. 2019 Jun 16. pii: RA119.008889. doi: 10.1074/jbc.RA119.008889. PMID:31209106 doi:http://dx.doi.org/10.1074/jbc.RA119.008889

6ok1, resolution 1.70Å

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