Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability (Q27748141)

2

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M Grättinger

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K Zaiss

4

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H Schurig

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R Jaenicke

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U Jacob

Structure of horse muscle phosphoglycerate kinase. Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 angstrom Fourier map.

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publication date

15 November 1997

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published in

Structure

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volume

5

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page(s)

1475-83

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issue

11

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cites work

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Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme

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Enzyme-Catalyzed Phosphoryl Transfer Reactions

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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

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The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent

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The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution

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Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima

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How to make my blood boil

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