2c44
From Proteopedia
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CRYSTAL STRUCTURE OF E. COLI TRYPTOPHANASE
Overview
Pyridoxal 5'-phosphate (PLP) dependent tryptophanase has been isolated, from Escherichia coli and its crystal structure has been determined. The, structure shares the same fold with and has similar quaternary structure, to Proteus vulgaris tryptophanase and tyrosine-phenol lyase, but is found, in a closed conformation when compared with these two enzymes. The, tryptophanase structure, solved in its apo form, does not have covalent, PLP bound in the active site, but two sulfate ions. The sulfate ions, occupy the phosphoryl-binding site of PLP and the binding site of the, alpha-carboxyl of the natural substrate tryptophan. One of the sulfate, ions makes extensive interactions with both the transferase and, PLP-binding domains of the protein and appears to be responsible for, holding the ... [(full description)]
About this Structure
2C44 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 and K as [ligands]. Active as [Tryptophanase], with EC number [4.1.99.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of Escherichia coli tryptophanase., Ku SY, Yip P, Howell PL, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):814-23. Epub 2006, Jun 20. PMID:16790938
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