2tpl
From Proteopedia
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TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION
Overview
The X-ray structure of tyrosine phenol-lyase (TPL) complexed with a, substrate analog, 3-(4'-hydroxyphenyl)propionic acid, shows that Arg 381, is located in the substrate binding site, with the side-chain NH1 4.1 A, from the 4'-OH of the analog. The structure has been deduced at 2.5 A, resolution using crystals that belong to the P2(1)2(1)2 space group with a, = 135.07 A, b = 143.91 A, and c = 59.80 A. To evaluate the role of Arg 381, in TPL catalysis, we prepared mutant proteins replacing arginine with, alanine (R381A), with isoleucine (R381I), and with valine (R381V). The, beta-elimination activity of R381A TPL has been reduced by 10(-4)-fold, compared to wild type, whereas R381I and R381V TPL exhibit no detectable, beta-elimination activity with L-tyrosine as substrate. However, R381A, ... [(full description)]
About this Structure
2TPL is a [Single protein] structure of sequence from [Citrobacter freundii] with CS and HPP as [ligands]. Active as [Lyase], with EC number [4.1.99.2]. Structure known Active Sites: CS and PLP. Full crystallographic information is available from [OCA].
Reference
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity., Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS, Biochemistry. 1997 May 27;36(21):6502-10. PMID:9174368
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