TAILIEUCHUNG - Báo cáo khoa học: Large conformational changes in the Escherichia coli tryptophan synthase b2 subunit upon pyridoxal 5¢-phosphate binding

To understand the basis for the lower activity of the tryptophan synthaseb2 subunit in comparison to thea2b2 complex, we determined the crystal struc-tures of apo-b2 and holo-b2 from Escherichia coliat and A˚ resolu-tions, respectively. To our knowledge, this is the first report of both b2 subunit structures with and without pyridoxal-5¢-phosphate. | ỊFEBS Journal Large conformational changes in the Escherichia coli tryptophan synthase p2 subunit upon pyridoxal 5 -phosphate binding Kazuya Nishio1 Kyoko Ogasahara1 Yukio Morimoto2 3 Tomitake Tsukihara1 4 Soo Jae Lee5 and Katsuhide Yutani3 1 Institute for Protein Research Osaka University Japan 2 Research Reactor Institute Kyoto University Japan 3 RIKEN SPring-8 Center Harima Institute Japan 4 Department of Life Science University of Hyogo Japan 5 College of Pharmacy Chungbuk NationalUniversity Korea Keywords apo- and holo-forms conformationalchange PLP-binding tryptophan synthase b2 subunit X-ray crystal structure Correspondence Katsuhide Yutani RIKEN SPring-8 Center Harima Institute 1-1-1 Kouto Sayo Hyogo 679-5148 Japan Fax 81-791-58-2917 Tel 81-791-58-2937 E-mail yutani@ Soo Jae Lee College of Pharmacy Chungbuk NationalUniversity Sungbong-ro 410 Cheongju Chungbuk Korea Fax 82-43-268-2732 Tel 82-43-261-2816 E-mail sjlee@ Database Structural data are available from the Protein Data Bank under the accession codes for the holo- 2DH5 and apo- 2DH6 forms Received 16 October 2009 revised 24 February 2010 accepted 1 March 2010 doi To understand the basis for the lower activity of the tryptophan synthase b2 subunit in comparison to the a2p2 complex we determined the crystal structures of apo-b2 and holo-b2 from Escherichia coll at and TA resolutions respectively. To our knowledge this is the first report of both b2 subunit structures with and without pyridoxal-5 -phosphate. The apo-type molecule retained a dimeric form in solution as in the case of the holo-b2 subunit. The subunit structures of both the apo-b2 and the holo-b2 forms consisted of two domains namely the N domain and the C domain. Although there were significant structural differences between the apo- and holo-structures they could be easily superimposed with a 22 rigid body rotation of the C domain. The pyridoxal-5 -phosphate-bound .

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