scholarly journals The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1

1989 ◽  
Vol 260 (3) ◽  
pp. 857-862 ◽  
Author(s):  
D N Nunn ◽  
D Day ◽  
C Anthony

The nucleotide and deduced amino acid sequence of a novel small (beta) subunit of methanol dehydrogenase of Methylobacterium extorquens AM1 (previously Pseudomonas AM1) has been determined. Work with the whole protein has shown that is has an alpha 2 beta 2 configuration.

1988 ◽  
Vol 256 (2) ◽  
pp. 673-676 ◽  
Author(s):  
D N Nunn ◽  
C Anthony

The nucleotide sequence and deduced amino acid sequence of the cytochrome cL of Methylobacterium extorquens (Pseudomonas AM1; Methylobacterium AM1) shows that this cytochrome c is completely different, except for its haem-binding site, from all other cytochromes.


1991 ◽  
Vol 266 (17) ◽  
pp. 11009-11016 ◽  
Author(s):  
D.J. Erle ◽  
C. Rüegg ◽  
D. Sheppard ◽  
R. Pytela

1987 ◽  
Vol 105 (3) ◽  
pp. 1183-1190 ◽  
Author(s):  
W S Argraves ◽  
S Suzuki ◽  
H Arai ◽  
K Thompson ◽  
M D Pierschbacher ◽  
...  

The amino acid sequence deduced from cDNA of the human placental fibronectin receptor is reported. The receptor is composed of two subunits: an alpha subunit of 1,008 amino acids which is processed into two polypeptides disulfide bonded to one another, and a beta subunit of 778 amino acids. Each subunit has near its COOH terminus a hydrophobic segment. This and other sequence features suggest a structure for the receptor in which the hydrophobic segments serve as transmembrane domains anchoring each subunit to the membrane and dividing each into a large ectodomain and a short cytoplasmic domain. The alpha subunit ectodomain has five sequence elements homologous to consensus Ca2+-binding sites of several calcium-binding proteins, and the beta subunit contains a fourfold repeat strikingly rich in cysteine. The alpha subunit sequence is 46% homologous to the alpha subunit of the vitronectin receptor. The beta subunit is 44% homologous to the human platelet adhesion receptor subunit IIIa and 47% homologous to a leukocyte adhesion receptor beta subunit. The high degree of homology (85%) of the beta subunit with one of the polypeptides of a chicken adhesion receptor complex referred to as integrin complex strongly suggests that the latter polypeptide is the chicken homologue of the fibronectin receptor beta subunit. These receptor subunit homologies define a superfamily of adhesion receptors. The availability of the entire protein sequence for the fibronectin receptor will facilitate studies on the functions of these receptors.


2011 ◽  
Vol 193 (21) ◽  
pp. 6032-6038 ◽  
Author(s):  
E. Skovran ◽  
A. D. Palmer ◽  
A. M. Rountree ◽  
N. M. Good ◽  
M. E. Lidstrom

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