Homocitrate synthase: Difference between revisions

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{{STRUCTURE_3ivt|  PDB=3ivt | SIZE=400| SCENE= |right|CAPTION=Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions [[3ivt]] }}
<StructureSection load='3ivt' size='400' side='right' scene='46/465446/Cv/1' caption='Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions [[3ivt]]'>
 
== Function ==
== Function ==
'''Homocitrate synthase''' (HS) participates in lysine biosynthesis and pyruvate metabolism.  HS catalyzes the conversion of acetyl-CoA + H2O + 2-oxoglutarate to 2-hydroxybutane-1,2,4-tricarboxylate + CoA<ref>PMID:5836514</ref>.
'''Homocitrate synthase''' (HS) participates in lysine biosynthesis and pyruvate metabolism.  HS catalyzes the conversion of acetyl-CoA + H2O + 2-oxoglutarate to 2-hydroxybutane-1,2,4-tricarboxylate + CoA<ref>PMID:5836514</ref>.


== Structural highlights ==
== Structural highlights ==
The HS active site is located in the interior of the N-terminal TIM-barrel domain. The metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate<ref>PMID:19776021</ref>.  
The HS <scene name='46/465446/Cv/7'>active site is located in the interior of the N-terminal TIM-barrel domain</scene>.
 
*<scene name='46/465446/Cv/8'>Active site</scene>.  
*The <scene name='46/465446/Cv/9'>metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate</scene><ref>PMID:19776021</ref>. Water molecules shown as red spheres.  
</StructureSection>
== 3D Structures of homocitrate synthase ==
== 3D Structures of homocitrate synthase ==


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[[2zyf]] - TtHS + α-ketoglutarate + Mg<br />
[[2zyf]] - TtHS + α-ketoglutarate + Mg<br />
[[2ztk]] – TtHS + homocitrate<br />
[[2ztk]] – TtHS + homocitrate<br />
[[3a9i]] – TtHS + lysine
[[3a9i]] – TtHS + lysine<br />
[[6ktq]] - HS + -ketoglutarate + CoA – ''Sulfolobus acidocaldarius''<br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]