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Nature Structural & Molecular Biology (4)

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Advanced filters: Author: Allan Matte Clear advanced filters

Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg²⁺–oxalate ternary complex of Escherichia coli PEP carboxykinase

Leslie W. Tari
Allan Matte
Louis T.J. Delbaere
Research01 Apr 1996
Nature Structural Biology

Volume: 3, P: 355-363
Mg²⁺–Mn²⁺ clusters in enzyme-catalyzed phosphoryl-transfer reactions

Here we show how Mg²⁺ and Mn²⁺ function in Escherichia coli phosphoenolpyruvate carboxykinase (PCK) and we propose a general model for the role of binuclear metal clusters in enzyme-catalyzed phosphoryl-transfer reactions.

Leslie W. Tari
Allan Matte
Louis T.J. Delbaere
Correspondence01 Dec 1997
Nature Structural Biology

Volume: 4, P: 990-994
Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP

J. Sivaraman
Véronique Sauvé
Allan Matte
Research15 Apr 2002
Nature Structural Biology

Volume: 9, P: 353-358
Bacterial polysaccharide co-polymerases share a common framework for control of polymer length

Ante Tocilj
Christine Munger
Miroslaw Cygler
Research20 Jan 2008
Nature Structural & Molecular Biology

Volume: 15, P: 130-138

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Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg2+–oxalate ternary complex of Escherichia coli PEP carboxykinase

Mg2+–Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions

Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP

Bacterial polysaccharide co-polymerases share a common framework for control of polymer length

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Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg²⁺–oxalate ternary complex of Escherichia coli PEP carboxykinase

Mg²⁺–Mn²⁺ clusters in enzyme-catalyzed phosphoryl-transfer reactions