2.0 Å resolution structure of a ternary complex of pig muscle phosphoglycerate kinase containing 3-phospho-D-glycerate and the nucleotide Mn adenylylimidodiphosphate

1996 ◽  
Vol 24 (3) ◽  
pp. 292-303 ◽  
Author(s):  
Andrew May ◽  
Maria Vas ◽  
Karl Harlos ◽  
Colin Blake
Keyword(s):  
Ternary Complex ◽  
Phosphoglycerate Kinase ◽  
Pig Muscle ◽  
Resolution Structure

scholarly journals Incomplete refolding of a fragment of the N-terminal domain of pig muscle 3-phosphoglycerate kinase that lacks a subdomain

2001 ◽  
Vol 268 (6) ◽  
pp. 1851-1860 ◽  
Author(s):  
Andrea N. Szilágyi ◽  
Nina V. Kotova ◽  
Gennady V. Semisotnov ◽  
Mária Vas
Keyword(s):  
Phosphoglycerate Kinase ◽  
Terminal Domain ◽  
Pig Muscle

Immobilization of pig muscle 3-phosphoglycerate kinase

1985 ◽  
Vol 7 (7) ◽  
pp. 357-360 ◽  
Author(s):  
L.M. Simon ◽  
J. Szelei ◽  
B. Szajáni ◽  
L. Boross
Keyword(s):  
Phosphoglycerate Kinase ◽  
Pig Muscle

scholarly journals Insights into Base Selectivity from the 1.8 Å Resolution Structure of an RB69 DNA Polymerase Ternary Complex

Biochemistry ◽  
2011 ◽  
Vol 50 (4) ◽  
pp. 581-590 ◽  
Author(s):  
Mina Wang ◽  
Shuangluo Xia ◽  
Gregor Blaha ◽  
Thomas A. Steitz ◽  
William H. Konigsberg ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Ternary Complex ◽  
Resolution Structure

Low Resolution Structure of Yeast Phosphoglycerate Kinase

1972 ◽  
Vol 240 (100) ◽  
pp. 134-136 ◽  
Author(s):  
P. L. WENDELL ◽  
T. N. BRYANT ◽  
H. C. WATSON
Keyword(s):  
Phosphoglycerate Kinase ◽  
Low Resolution ◽  
Resolution Structure

Structural dynamics of yeast hexokinase during catalysis

1981 ◽  
Vol 293 (1063) ◽  
pp. 43-52 ◽  
Keyword(s):  
Conformational Changes ◽  
Ternary Complex ◽  
Crystal Form ◽  
Low Resolution ◽  
Enzymatic Mechanism ◽  
Complex Crystals ◽  
And Control ◽  
Yeast Hexokinase ◽  
Resolution Structure

The binding of the substrate glucose to yeast hexokinase results in a substantial enzyme conformational change that is essential for catalysis and may be important for the enzyme’s specificity, as well as the control of its activity. From high-resolution crystal structures of the monomeric enzyme crystallized both in the presence and in the absence of glucose, we find that glucose binds into the deep cleft that separates the molecule into two lobes and causes these two lobes to move together and close off the cleft. The structure of the hexokinase crystallized in the presence of xylose and ADP is being determined at low resolution. In this crystal form, the enzyme was thought to be in the conformation of the ternary complex. However, a low-resolution structure of this crystal form shows clearly that the enzyme is in the ‘open’ form and is not a ternary complex. Crystals of the A isozyme with glucose and ADP may be. Further, chemically sequenced tryptic peptides are being incorporated into the model obtained by crystallographic refinement at 2.1 Å resolution. Completion of the sequence and the structure of the ternary complex should allow a detailed description of the enzymatic mechanism of this kinase and the role of substrate-induced conformational changes in catalysis and control.

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