Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state.

Sträter, Norbert; Håkansson, Kjell; Schnappauf, Georg; Braus, Gerhard H.; Lipscomb, William N.

doi:10.1073/pnas.93.8.3330

Cited by 48 publications

(71 citation statements)

References 15 publications

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“…A comparable loop does not exist in ScCM, which uses an arginine positioned approximately where Gly-149 of AtCM1 is located to provide a similar binding contact (10). This remodeling of the effector site may facilitate recognition of phenylalanine by AtCM1, as the AtCM1 R79K mutant shows decreased affinity for both phenylalanine and tyrosine ( Table 3).…”

Section: Discussionmentioning

confidence: 99%

“…5B). Thus, AtCM1 likely uses a catalytic mechanism involving transition state stabilization by Arg-229 and Lys-240, as described for the yeast enzyme (10). In addition, the overall structures of the AtCM1⅐tyrosine and AtCM1⅐phenylalanine complexes closely resemble the T-state of the yeast enzyme.…”

Section: Discussionmentioning

confidence: 99%

“…First, phenylalanine has no effect on ScCM (12,13). In the ScCM⅐tyrosine complex, Thr-145 forms a hydrogen bond with the tyrosine hydroxyl and seems to be important for tyrosine binding (10). In AtCM1, this residue is Val-217.…”

Section: Discussionmentioning

confidence: 99%

“…For example, the effector site of Saccharomyces cerevisiae chorismate mutase (ScCM) 3 can bind either tryptophan or tyrosine (10). Tryptophan binding activates ScCM, and tyrosine leads to attenuation of prephenate synthesis.…”

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confidence: 99%

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Structural Evolution of Differential Amino Acid Effector Regulation in Plant Chorismate Mutases

Westfall

Jez

2014

Journal of Biological Chemistry

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Background: Chorismate mutase is essential for aromatic amino acid biosynthesis. Results: Structural and biochemical studies of three chorismate mutases from Arabidopsis reveal distinct sets of effector molecules. Conclusion: Key residues in the effector site modulate the regulatory effects of ligands. Significance: Evolution of effector control may lead to specialized regulation of this enzyme in plants.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Structural Evolution of Differential Amino Acid Effector Regulation in Plant Chorismate Mutases

Westfall

Jez

2014

Journal of Biological Chemistry

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“…Several high resolution structures of CM have been recently reported, including CM structures from Escherichia coli (Lee and Saier, 1983), Bacillus subtilis (Chook et al, 1994), Saccharomyces cerevisiae (Strater et al, 1996;Strater et al, 1997;Xue et al, 1994), Thermus thermophilus (Helmstaedt et al, 2004) and Mycobacterium tuberculosis (Qamra et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Structures of open (R) and close (T) states of prephenate dehydratase (PDT)—Implication of allosteric regulation by l-phenylalanine

Tan

Zhang

et al. 2008

Journal of Structural Biology

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The enzyme prephenate dehydratase (PDT) converts prephenate to phenylpyruvate in Lphenylalanine biosynthesis. PDT is allosterically regulated by L-Phe and other amino acids. We report the first crystal structures of PDT from Staphylococcus aureus in a relaxed (R) state and PDT from Chlorobium tepidum in a tense (T) state. The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization. Both enzymes are tetramers (dimer of dimers) in crystal and solution while a PDT dimer can be regarded as a basic catalytic unit. The N-terminal PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In one PDT dimer two clefts are aligned to form an extended active site across the dimer interface. Similarly at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation.

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Electrostatics, allostery, and activity of the yeast chorismate mutase

Lin

et al. 1998

Proteins

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The predicted active site of chorismate mutase of baker's yeast Saccharomyces cerevisiae has been studied by continuum electrostatics, molecular surface/volume calculations, and molecular modeling. Our study shows that despite being subject to an allosteric transition, the enzyme's active-site pocket neither decreased in volume nor deformed significantly in shape between the active R state and the inactive T state. We find that the polar atmosphere in the pocket is responsible for the enzyme's affinity. A single amino acid, Glu23, can adequately account for the atmospheric variation. This residue swings into the active-site pocket from the R state to the T state. In the R state, Glu23 on helix H2 doubly pairs with Arg204 and Lys208 of H11, which is packed against H2. In the T state, a slide occurs between H11 and H2 such that Glu23 can no longer interact with Lys208 and competes with Asp24 for interacting with Arg204. Consequently, Glu23 is found in the T state to couple with Arg157, an active-site residue critical to substrate binding. The tandem sliding of H11 in both monomers profoundly changes the interactions in the dimer interface. The loop between H11 and H12 demonstrates the largest conformational change. Hence, we establish a connection between the allosteric transition and the activity of the enzyme. The conformational change in the transition is suggested to propagate into the active-site pocket via a series of polar interactions that result in polarity reversal in the active-site pocket, which regulates the enzyme's activity.

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Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state.

Abstract: The crystal structure of the tyrosine-bound T

Cited by 48 publications

References 15 publications

Structural Evolution of Differential Amino Acid Effector Regulation in Plant Chorismate Mutases

Structural Evolution of Differential Amino Acid Effector Regulation in Plant Chorismate Mutases

Structures of open (R) and close (T) states of prephenate dehydratase (PDT)—Implication of allosteric regulation by l-phenylalanine

Electrostatics, allostery, and activity of the yeast chorismate mutase

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