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Structure paper

TitleEnzyme-substrate complexes of allosteric citrate synthase: Evidence for a novel intermediate in substrate binding.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1834, Page 2546-2553, Year 2013
Publish dateFeb 18, 2013 (structure data deposition date)
AuthorsDuckworth, H.W. / Nguyen, N.T. / Gao, Y. / Donald, L.J. / Maurus, R. / Ayed, A. / Bruneau, B. / Brayer, G.D.
External linksBiochim. Biophys. Acta / PubMed:23954305
MethodsX-ray diffraction
Resolution1.9 - 2.7 Å
Structure data

PDB-4jad:
STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE from E. COLI
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4jae:
STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI complexed WITH S-CARBOXYMETHYL-COA
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4jaf:
STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI COMPLEXED with NADH
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4jag:
STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI COMPLEXED WITH oxaloacetate
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-CMC:
CARBOXYMETHYL COENZYME *A

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-OAA:
OXALOACETATE ION

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / CITRATE SYNTHASE / GRAM-NEGATIVE BACTERIA / ALLOSTERY / OXALOACETATE / ACETYLCOA / NADH / ALLOSTERIC ENZYME / TRICARBOXYLIC ACID CYCLE / ACETYL-COA / PROTEIN FOLDING / S-CARBOXYMETHYL-COA

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