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Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase fromEscherichia coli

✍ Scribed by Shumilin, Igor A.; Kretsinger, Robert H.; Bauerle, Ronald

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 262 KB
Volume: 24
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199603)24:3<404::aid-prot15>3.0.co;2-q

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✦ Synopsis

The phenylalanine-regulated isozyme of 3-deoxy-D-arabino-heptulosonate-7phosphate synthase (DAHPS) from Escherichia coli, its binary complexes with either substrate, phosphoenolpyruvate (PEP), or feedback inhibitor, Phe, and its ternary complexes with either PEP or Phe plus metal cofactor (either Mn2', Cd2', or Pb2+) were crystallized from polyethylglycol (PEG) solutions. All crystals of the DAHPS without Phe belong to space group C2, with cell parameters a = 213.5 A, b = 54.3 A, c = 149.0 A, p = 116.6'. All crystals of the enzyme with Phe also belong to space group C2, but with cell parameters a = 297.1 A, b = 91.4 A, c = 256.5 A, and p = 148.2'. o 1996 Wiey-Liss, Inc.

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