1wdw
From Proteopedia
(New page: 200px<br /><applet load="1wdw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wdw, resolution 3.00Å" /> '''Structural basis of ...) |
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| - | [[Image:1wdw.gif|left|200px]]<br /><applet load="1wdw" size=" | + | [[Image:1wdw.gif|left|200px]]<br /><applet load="1wdw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wdw, resolution 3.00Å" /> | caption="1wdw, resolution 3.00Å" /> | ||
'''Structural basis of mutual activation of the tryptophan synthase a2b2 complex from a hyperthermophile, Pyrococcus furiosus'''<br /> | '''Structural basis of mutual activation of the tryptophan synthase a2b2 complex from a hyperthermophile, Pyrococcus furiosus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the bifunctional tryptophan synthase | + | The three-dimensional structure of the bifunctional tryptophan synthase alpha(2)beta(2) complex from Pyrococcus furiosus was determined by crystallographic analysis. This crystal structure, with the structures of an alpha subunit monomer and a beta(2) subunit dimer that have already been reported, is the first structural set in which changes in structure that occur upon the association of the individual tryptophan synthase subunits were observed. To elucidate the structural basis of the stimulation of the enzymatic activity of each of the alpha and beta(2) subunits upon alpha(2)beta(2) complex formation, the conformational changes due to complex formation were analyzed in detail compared with the structures of the alpha monomer and beta(2) subunit dimer. The major conformational changes due to complex formation occurred in the region correlated with the catalytic function of the enzyme as follows. (1) Structural changes in the beta subunit were greater than those in the alpha subunit. (2) Large movements of A46 and L165 in the alpha subunit due to complex formation caused a more open conformation favoring the entry of the substrate at the alpha active site. (3) The major changes in the beta subunit were the broadening of a long tunnel through which the alpha subunit product (indole) is transferred to the beta active site and the opening of an entrance at the beta active site. (4) The changes in the conformations of both the alpha and beta subunits due to complex formation contributed to the stabilization of the subunit association, which is critical for the stimulation of the enzymatic activities. |
==About this Structure== | ==About this Structure== | ||
| - | 1WDW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] Full crystallographic information is available from [http:// | + | 1WDW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Tryptophan synthase]] | [[Category: Tryptophan synthase]] | ||
[[Category: Ishida, M.]] | [[Category: Ishida, M.]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S J.]] |
[[Category: Ma, J.]] | [[Category: Ma, J.]] | ||
[[Category: Nishio, K.]] | [[Category: Nishio, K.]] | ||
[[Category: Ogasahara, K.]] | [[Category: Ogasahara, K.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Tsukihara, T.]] | [[Category: Tsukihara, T.]] | ||
[[Category: Yamagata, Y.]] | [[Category: Yamagata, Y.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:43:12 2008'' |
Revision as of 13:43, 21 February 2008
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Structural basis of mutual activation of the tryptophan synthase a2b2 complex from a hyperthermophile, Pyrococcus furiosus
Overview
The three-dimensional structure of the bifunctional tryptophan synthase alpha(2)beta(2) complex from Pyrococcus furiosus was determined by crystallographic analysis. This crystal structure, with the structures of an alpha subunit monomer and a beta(2) subunit dimer that have already been reported, is the first structural set in which changes in structure that occur upon the association of the individual tryptophan synthase subunits were observed. To elucidate the structural basis of the stimulation of the enzymatic activity of each of the alpha and beta(2) subunits upon alpha(2)beta(2) complex formation, the conformational changes due to complex formation were analyzed in detail compared with the structures of the alpha monomer and beta(2) subunit dimer. The major conformational changes due to complex formation occurred in the region correlated with the catalytic function of the enzyme as follows. (1) Structural changes in the beta subunit were greater than those in the alpha subunit. (2) Large movements of A46 and L165 in the alpha subunit due to complex formation caused a more open conformation favoring the entry of the substrate at the alpha active site. (3) The major changes in the beta subunit were the broadening of a long tunnel through which the alpha subunit product (indole) is transferred to the beta active site and the opening of an entrance at the beta active site. (4) The changes in the conformations of both the alpha and beta subunits due to complex formation contributed to the stabilization of the subunit association, which is critical for the stimulation of the enzymatic activities.
About this Structure
1WDW is a Protein complex structure of sequences from Pyrococcus furiosus with as ligand. Active as Tryptophan synthase, with EC number 4.2.1.20 Full crystallographic information is available from OCA.
Reference
Conformational Changes in the tryptophan synthase from a hyperthermophile upon alpha2beta2 complex formation: crystal structure of the complex., Lee SJ, Ogasahara K, Ma J, Nishio K, Ishida M, Yamagata Y, Tsukihara T, Yutani K, Biochemistry. 2005 Aug 30;44(34):11417-27. PMID:16114878
Page seeded by OCA on Thu Feb 21 15:43:12 2008
Categories: Protein complex | Pyrococcus furiosus | Tryptophan synthase | Ishida, M. | Lee, S J. | Ma, J. | Nishio, K. | Ogasahara, K. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Tsukihara, T. | Yamagata, Y. | Yutani, K. | PLP | Alpha+beta | Alpha/beta | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
