Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

Hyde, C. Craig; Ahmed, Salman; Padlan, Eduardo A.; Miles, Edith Wilson; Davies, David R.

doi:10.1016/s0021-9258(19)77913-7

Cited by 743 publications

(422 citation statements)

References 81 publications

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“…The central region could be predicted to constitute the ~ interactive site. With the advent of recent X-ray crystallographic studies (Hyde et al, 1988), which have identified the regions contacting ~ to be part of the central region, this inference derived from early mutational studies is confirmed.…”

Section: Location Of Interacflve and Catalytic Sitesmentioning

confidence: 85%

“…This suggests that there are also key interactive residues that remain unchanged in many of the mutation studies. Furthermore, as a~ interaction occurs over a relatively large area (1190 A2 of a and 1110 A2 of ~; Hyde et al, 1988), in comparison to that of the Iysozyme-anti-Iysozyme reported surface of interaction (750 A2, Sherriff et al, 1987; and 690 A2, Amit et al, 1986), residues at the overlap may give a small, but observable interaction effect. Mutational studies, therefore, have identified residues affecting the strength of interaction through effects on association constants and ~2 enhancement.…”

Section: Location Of Interacflve and Catalytic Sitesmentioning

confidence: 94%

“…The overall structure of the tetrameric complex is an extended (X~~(X subunit arrangement with an overall length of 150 A (Hyde et al, 1988). The…”

Section: Mechanisms Of Regulating Tryptophan Biosynthesismentioning

confidence: 99%

“…It is not surprising that an area of overlap has been demonstrated. Hyde et al (1988) described the channelling of indole from the a active site to that of ~ via the indole tunnel. The tunnel begins at the a active site and must pass through the interactive region before reaching the ~ active site.…”

Section: Location Of Interacflve and Catalytic Sitesmentioning

confidence: 99%

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7 The Molecular Biology of Tryptophan Synthase: A Model for Protein–Protein Interaction

Swift

Stewart

1991

Biotechnology and Genetic Engineering Reviews

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Review objectivesOne of the major goals of modem biochemistry is to elucidate the molecular mechanisms which operate within protein structure/folding to promote the specific interaction of disparate subunits in multisubunit enzyme formation. One perspective recognizes that many of the keys to protein-protein interaction may be elucidated through the detailed understanding of a few model systems. Implicit in this view is the belief that there are a limited number of molecular motifs available for interprotein recognition, that these may be defined from limited studies and that the enormous diversity of protein interaction reflects the numerical consequence of randomly permutating a modest number of structural motifs. With the advent of protein engineering, the elucidation of these elements is of considerable importance. The opportunity to design protein interaction by conforming to a limited set of rules, would have far-reaching consequences in the development of biotechnology. The tryptophan synthase system has been the subject of a number of recent reviews. These have concentrated mainly on enzymology (Miles, 1986;Miles, Bauerle and Ahmed, 1987), evolutionary aspects (Crawford, 1989) and the early history of the biochemical studies with tryptophan synthase (Yanofsky, 1987), how the enzyme was characterized and its role in the determination of gene-protein co-linearity and the genetic code. We believe that a considerable resource for the pursuance of protein structure/folding studies is available in the wealth of molecular and biochemical data on tryptophan synthase

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Section: Location Of Interacflve and Catalytic Sitesmentioning

confidence: 85%

Section: Location Of Interacflve and Catalytic Sitesmentioning

confidence: 94%

“…The overall structure of the tetrameric complex is an extended (X~~(X subunit arrangement with an overall length of 150 A (Hyde et al, 1988). The…”

Section: Mechanisms Of Regulating Tryptophan Biosynthesismentioning

confidence: 99%

Section: Location Of Interacflve and Catalytic Sitesmentioning

confidence: 99%

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7 The Molecular Biology of Tryptophan Synthase: A Model for Protein–Protein Interaction

Swift

Stewart

1991

Biotechnology and Genetic Engineering Reviews

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“…Each catalytic intermediate is characterized by a distinct absorption spectrum and, presumably, by a distinct conformation (Houben & Dunn 1990). The structure of the enzyme from Salmonella (strain TB2211) has been determined (Hyde et al 1988). Microcrystals of the enzyme are catalytically active and do not break in the course of steady-state reactions (Ahmed et al 1987).…”

Section: (D) Tryptophan Synthasementioning

confidence: 99%

Time course of chemical and structural events in protein crystals measured by microspectrophotometry

Rossi

Mozzarelli

Peracchi

et al. 1992

Phil. Trans. R. Soc. Lond. A

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The functional properties of proteins in the crystalline state have been investigated over the past 30 years by a variety of methods, including single crystal polarized absorption spectroscopy. This technique has provided information on the accumulation and equilibrium distribution of protein-ligand complexes in the crystal and, in a few cases, on the rates of interconversion of catalytic intermediates. It has been possible to detect synergistic effects in the binding of different ligands, cooperativity and half-site reactivity and even formation of active multiprotein complexes, obtained by diffusion of one small protein in the pre-formed crystals of the other. Lattice interactions restrain the conformational transitions of some proteins existing in multiple states in solution. The crystal offers the unique opportunity to analyse not only the structure but also the function of a single form of the protein. The relevance of these data to the planning and interpretation of structural studies, especially in the perspectives of time-resolved crystallography, will be discussed with reference to well-characterized systems.

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Secondary structure prediction and unrefined tertiary structure prediction for cyclin A, B, and D

Gerloff¹,

Cohen²

1996

Proteins

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Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

Cited by 743 publications

References 81 publications

7 The Molecular Biology of Tryptophan Synthase: A Model for Protein–Protein Interaction

7 The Molecular Biology of Tryptophan Synthase: A Model for Protein–Protein Interaction

Time course of chemical and structural events in protein crystals measured by microspectrophotometry

Secondary structure prediction and unrefined tertiary structure prediction for cyclin A, B, and D

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