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2.3.3.8: ATP citrate synthase

This is an abbreviated version!
For detailed information about ATP citrate synthase, go to the full flat file.

Word Map on EC 2.3.3.8

Reaction

ADP
+
phosphate
 +
acetyl-CoA
 +
oxaloacetate
=
ATP
 +
citrate
 +
CoA

Synonyms

ACL, ACL1, ACL2, ACLA, ACLB, ACLY, adenosine triphosphate citrate lyase, ATP citrate (pro-S)-lyase, ATP citrate lyase, ATP citrate lyase isoform 2, ATP-citrate lyase, ATP-citrate synthase A-2, ATP-citrate synthase alpha chain protein 2, ATP-citric lyase, ATP:citrate lyase, ATP:citrate oxaloacetate lyase ((pro-3S)-CH2COO--> acetyl-CoA) (ATP-dephosphorylating), ATP:citrate oxaloacetate-lyase (pro-3S-CH2COO->acetyl-CoA, ATP dephosphorylating), ATP:citrate oxaloacetate-lyase CoA-acetylating and ATP-dephosphorylating, Citrate cleavage enzyme, citrate-ATP lyase, citric cleavage enzyme, Earlier Degraded Tapetum1, EC 4.1.3.8, EDT1, Os11g0696200

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.8 ATP citrate synthase

Crystallization

Crystallization on EC 2.3.3.8 - ATP citrate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour diffusion crystallization
full structure of human ACLY homotetramer in ternary complex with the inhibitor and ADP with an overall resolution of 3.67 A
in complex with citrate or tartrate, hanging drop vapor diffusion method, using either 12.5% (w/v) PEG 3350, 100 mM sodium tartrate, 100 mM Tris-HCl (pH 7.0) for the native protein or 10% PEG 3350, 75 mM potassium citrate, 100 mM Tris-HCl (pH 7.0) for the selenomethionyl protein
in the presence of tartrate, ATP and magnesium ions
-
tartrate and ADP-Mg2+ bound N-terminal portion of the enzyme containing residues 1-817, hanging drop vapor diffusion method, using 12.5% (w/v) polyethylene glycol 3350, 125 mM sodium tartrate, 100 mM Tris-HCl (pH 8.2)
vapour diffusion crystallization
vapour diffusion in hanging drops. The protein is modified by introducing cleavage sites for Tobacco etch virus protease on either side of a disordered linker. The protein crystallized consists of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. When co-crystals are grown with ATP and magnesium ions as well as either the inhibitor (2S,3S)-2-hydroxycitrate or citrate, Mg2+-ADP is bound and His760 is phosphorylated