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Crystallization of the Malonyl Coenzyme A-Acyl Carrier Protein Transacylase from Escherichia coli

1994; Elsevier BV; Volume: 242; Issue: 1 Linguagem: Inglês

10.1006/jmbi.1994.1559

1089-8638

Laurence Serre, Lora Swenson, Ruth Green, Yunju Wei, Ira I. G. S. Verwoert, Elizabeth C. Verbree, Antoine R. Stuitje, Zygmunt S. Derewenda,

Click Chemistry and Applications

The malonyl coenzyme A-acyl protein transacylase, a single polypeptide chain of 358 amino acid residues and a molecular mass of 32 kDa, is a key component of the fatty acid synthase multienzyme complex. The elucidation of its three-dimensional structure will help in the understanding of the molecular basis of the biosynthesis of fatty acids, as well as of polyketides and related biologically active molecules. Three X-ray-quality crystal forms of the Escherichia coli fabD gene product encoding for malonyl coenzyme A-acyl carrier protein transacylase have been obtained using the hanging-drop method and ammonium sulfate as precipitant. Two are tetragonal and each contains two molecules in the asymmetric unit (form I: space group P 43(1)212 with a = b = 83?9 Å, c = 166?5 Å and form II: space group P4 with a = b = 132?64 Å, c = 38?85 Å), whereas the third form belongs to the hexagonal system and contains one molecule in the asymmetric unit (space group P61(5) with a = b = 68?52 Å, c = 117?71 Å). In each case, the diffraction pattern extends to approximately 2?0 Å resolution using CuKα radiation from a rotating anode source.