1ax4

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spinqualitylabelsall models 1ax4, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

TRYPTOPHANASE FROM PROTEUS VULGARIS

Overview

The X-ray structure of tryptophanase (Tnase) reveals the interactions, responsible for binding of the pyridoxal 5'-phosphate (PLP) and atomic, details of the K+ binding site essential for catalysis. The structure of, holo Tnase from Proteus vulgaris (space group P2(1)2(1)2(1) with a = 115.0, A, b = 118.2 A, c = 153.7 A) has been determined at 2.1 A resolution by, molecular replacement using tyrosine phenol-lyase (TPL) coordinates. The, final model of Tnase, refined to an R-factor of 18.7%, (Rfree = 22.8%), suggests that the PLP-enzyme from observed in the structure is a, ketoenamine. PLP is bound in a cleft formed by both the small and large, domains of one subunit and the large domain of the adjacent subunit in the, so-called "catalytic" dimer. The K+ cations are located on the ... [(full description)]

About this Structure

1AX4 is a [Single protein] structure of sequence from [Proteus vulgaris] with K as [ligand]. Active as [Tryptophanase], with EC number [4.1.99.1]. Structure known Active Sites: LPA, LPB, LPC, LPD, POA, POB, POC and POD. Full crystallographic information is available from [OCA].

Reference

Crystal structure of tryptophanase., Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH, J Mol Biol. 1998 Feb 27;276(3):603-23. PMID:9551100

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