Evidence for a nucleotide binding site on the isolated .beta. subunit from Escherichia coli F1-ATPase. Interaction between nucleotide and aurovertin D binding sites

Biochemistry ◽  
1984 ◽  
Vol 23 (26) ◽  
pp. 6591-6595 ◽  
Author(s):  
Jean Paul Issartel ◽  
Pierre V. Vignais
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Beta Subunit ◽  
F1 Atpase

scholarly journals Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by31P NMR Spectroscopy

2011 ◽  
Vol 32 (2) ◽  
pp. 531-535 ◽  
Author(s):  
Nam-Kung Jun ◽  
Joon-Hyung Sohn ◽  
Byung-Il Yeh ◽  
Jong-Whan Choi ◽  
Hyun-Won Kim
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites

The Nucleotide-Binding Site of the Escherichia coli DnaC Protein: Molecular Topography of DnaC Protein–Nucleotide Cofactor Complexes

2005 ◽  
Vol 43 (3) ◽  
pp. 331-354 ◽  
Author(s):  
Roberto Galletto ◽  
Maria J. Jezewska ◽  
Rodrigo Maillard ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Dnac Protein

Measurement of site occupancy and rotation speed of F1-ATPase without noncatalytic nucleotide binding site

2003 ◽  
Vol 43 (supplement) ◽  
pp. S134
Author(s):  
R. Kon-Shimo ◽  
E. Muneyuki ◽  
K. Iai ◽  
N. Sakaki ◽  
K. Adachi ◽  
...  
Keyword(s):  
Binding Site ◽  
Rotation Speed ◽  
Site Occupancy ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
F1 Atpase

Photoaffinity labelling of a low-affinity nucleotide binding site on the β-subunit of yeast mitochondrial F1 -ATPase

FEBS Letters ◽  
1979 ◽  
Vol 108 (1) ◽  
pp. 253-256 ◽  
Author(s):  
Roland Gregory ◽  
Diether Recktenwald ◽  
Benno Hess ◽  
Hans-Jochen Schäfer ◽  
Peter Scheurich ◽  
...  
Keyword(s):  
Binding Site ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Β Subunit ◽  
Photoaffinity Labelling ◽  
F1 Atpase

scholarly journals Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site.

1986 ◽  
Vol 5 (6) ◽  
pp. 1351-1358 ◽  
Author(s):  
J. Tucker ◽  
G. Sczakiel ◽  
J. Feuerstein ◽  
J. John ◽  
R.S. Goody ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
P21 Proteins

scholarly journals The Nucleotide-binding Site of Human Sphingosine Kinase 1

2002 ◽  
Vol 277 (51) ◽  
pp. 49545-49553 ◽  
Author(s):  
Stuart M. Pitson ◽  
Paul A. B. Moretti ◽  
Julia R. Zebol ◽  
Reza Zareie ◽  
Claudia K. Derian ◽  
...  
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Sphingosine Kinase ◽  
Structural Similarity ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Site Directed Mutagenesis ◽  
Sequence Motifs ◽  
Sphingosine Kinase 1 ◽  
Nucleotide Binding Sites

Sphingosine kinase catalyzes the formation of sphingosine 1-phosphate, a lipid second messenger that has been implicated in a number of agonist-driven cellular responses including mitogenesis, anti-apoptosis, and expression of inflammatory molecules. Despite the importance of sphingosine kinase, very little is known regarding its structure or mechanism of catalysis. Moreover, sphingosine kinase does not contain recognizable catalytic or substrate-binding sites, based on sequence motifs found in other kinases. Here we have elucidated the nucleotide-binding site of human sphingosine kinase 1 (hSK1) through a combination of site-directed mutagenesis and affinity labeling with the ATP analogue, FSBA. We have shown that Gly82of hSK1 is involved in ATP binding since mutation of this residue to alanine resulted in an enzyme with an ∼45-fold higherKm(ATP). We have also shown that Lys103is important in catalysis since an alanine substitution of this residue ablates catalytic activity. Furthermore, we have shown that this residue is covalently modified by FSBA. Our data, combined with amino acid sequence comparison, suggest a motif of SGDGX17–21K is involved in nucleotide binding in the sphingosine kinases. This motif differs in primary sequence from all previously identified nucleotide-binding sites. It does, however, share some sequence and likely structural similarity with the highly conserved glycine-rich loop, which is known to be involved in anchoring and positioning the nucleotide in the catalytic site of many protein kinases.

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