Synergistic Regulation and Ligand-Induced Conformational Changes of Tryptophan Synthase

Biochemistry ◽  
2009 ◽  
Vol 48 (41) ◽  
pp. 9921-9931 ◽  
Author(s):  
M. Qaiser Fatmi ◽  
Rizi Ai ◽  
Chia-en A. Chang
Keyword(s):  
Conformational Changes ◽  
Tryptophan Synthase ◽  
Synergistic Regulation

Conformational Changes in the α-Subunit Coupled to Binding of the β2-Subunit of Tryptophan Synthase fromEscherichia coli:  Crystal Structure of the Tryptophan Synthase α-Subunit Alone†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (4) ◽  
pp. 1184-1192 ◽  
Author(s):  
Kazuya Nishio ◽  
Yukio Morimoto ◽  
Manabu Ishizuka ◽  
Kyoko Ogasahara ◽  
Tomitake Tsukihara ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Changes ◽  
Tryptophan Synthase ◽  
Α Subunit ◽  
Fromescherichia Coli

Conformational changes and subunit communication in tryptophan synthase: effect of substrates and substrate analogs

Biochemistry ◽  
1992 ◽  
Vol 31 (33) ◽  
pp. 7535-7542 ◽  
Author(s):  
Giovanni B. Strambini ◽  
Patrizia Cioni ◽  
Alessio Peracchi ◽  
Andrea Mozzarelli
Keyword(s):  
Conformational Changes ◽  
Tryptophan Synthase ◽  
Substrate Analogs ◽  
Subunit Communication

Large conformational changes in the Escherichia coli tryptophan synthase β2 subunit upon pyridoxal 5′-phosphate binding

FEBS Journal ◽  
2010 ◽  
Vol 277 (9) ◽  
pp. 2157-2170 ◽  
Author(s):  
Kazuya Nishio ◽  
Kyoko Ogasahara ◽  
Yukio Morimoto ◽  
Tomitake Tsukihara ◽  
Soo Jae Lee ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Conformational Changes ◽  
Tryptophan Synthase ◽  
Phosphate Binding

Crystal Structures of a Mutant (βK87T) Tryptophan Synthase α2β2Complex with Ligands Bound to the Active Sites of the α- and β-Subunits Reveal Ligand-Induced Conformational Changes‡

Biochemistry ◽  
1997 ◽  
Vol 36 (25) ◽  
pp. 7664-7680 ◽  
Author(s):  
Sangkee Rhee ◽  
Kevin D. Parris ◽  
C. Craig Hyde ◽  
S. Ashraf Ahmed ◽  
Edith Wilson Miles ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Changes ◽  
Active Sites ◽  
Tryptophan Synthase ◽  
Α And Β Subunits

Conformational Changes in the Tryptophan Synthase from a Hyperthermophile upon α2β2Complex Formation:  Crystal Structure of the Complex†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (34) ◽  
pp. 11417-11427 ◽  
Author(s):  
Soo Jae Lee ◽  
Kyoko Ogasahara ◽  
Jichun Ma ◽  
Kazuya Nishio ◽  
Masami Ishida ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Changes ◽  
Tryptophan Synthase

Influence of Calcium Ions on the Plant Cell Surface: Membrane Fusions and Conformational Changes

1974 ◽  
Vol 32 ◽  
pp. 154-155
Author(s):  
D. James Morré ◽  
Charles E. Bracker ◽  
William J. VanDerWoude
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Conformational Changes ◽  
Calcium Ions ◽  
Surface Membrane ◽  
Carboxyl Groups ◽  
Cross Linking ◽  
Ultrastructural Evidence ◽  
Glycine Max L ◽  
Wall Extensibility

Calcium ions in the concentration range 5-100 mM inhibit auxin-induced cell elongation and wall extensibility of plant stems. Inhibition of wall extensibility requires that the tissue be living; growth inhibition cannot be explained on the basis of cross-linking of carboxyl groups of cell wall uronides by calcium ions. In this study, ultrastructural evidence was sought for an interaction of calcium ions with some component other than the wall at the cell surface of soybean (Glycine max (L.) Merr.) hypocotyls.

Role of spectrin in membrane fusion and in shape change of human erythrocyte ghost

1978 ◽  
Vol 36 (2) ◽  
pp. 328-329
Author(s):  
Hideo Hayashi ◽  
Yoshikazu Hirai ◽  
John T. Penniston
Keyword(s):  
Conformational Changes ◽  
Human Erythrocyte ◽  
Shape Change ◽  
Membrane Surface ◽  
Slight Modification ◽  
Active Role ◽  
Main Role ◽  
Bank Blood ◽  
Human Erythrocyte Ghost

Spectrin is a membrane associated protein most of which properties have been tentatively elucidated. A main role of the protein has been assumed to give a supporting structure to inside of the membrane. As reported previously, however, the isolated spectrin molecule underwent self assemble to form such as fibrous, meshwork, dispersed or aggregated arrangements depending upon the buffer suspended and was suggested to play an active role in the membrane conformational changes. In this study, the role of spectrin and actin was examined in terms of the molecular arrangements on the erythrocyte membrane surface with correlation to the functional states of the ghosts.Human erythrocyte ghosts were prepared from either freshly drawn or stocked bank blood by the method of Dodge et al with a slight modification as described before. Anti-spectrin antibody was raised against rabbit by injection of purified spectrin and partially purified.

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