Words similar to midas
Example sentences for: midas
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The residues in the MIDAS motifs lie on three closely apposed loops located on the upper edge of the β-sheet, where they form the metal-binding site, with oxygen atoms in the aspartate, serine and threonine residues coordinating the metal ion [ 9 ] . In integrin α2β1, which is a collagen receptor, the metal-binding site also binds the collagen ligand through the conserved glutamate in a GFOGER motif (O = hydroxyproline) completing the coordination sphere of the metal [ 28 ] . In vivo, the binding of collagen at this site appears to be regulated through a conformational shift in which the loops forming the MIDAS site change from a closed to an open conformation [ 29 30 31 ] . Other proteins containing a domain with all three MIDAS motifs include the D-subunit of magnesium chelatase [ 32 ] , Ca-activated chloride-channel protein [ 33 34 ] , nitrate reductase (accession AAC79447), and the D subunit of nitric oxide reductase (accession AAC45374).
Wanniski, in other words, has committed the sin of King Midas: He has forgotten that gold is only a metal, and that its value comes only from the truly useful goods for which it can be exchanged.
All the MIDAS sequence motifs in this domain are retained and most of the residues in the highly conserved NH 2 -extension of the M-domain are unaffected.
The BchI subunit also possesses a single AAA protomer, but contains no MIDAS domain [ 32 ] . The third subunit BchH is able to bind the protoporphyrin ring in either the presence or absence of ATP.
The initial step of the insertion can proceed in the presence of either Mg.ATP or a non-hydrolyzable ATP-analog and involves oligomerization of the BchD and BchI subunits to form an oligomeric ring of AAA protomers that resembles the ring structure of NSF and other AAA proteins [ 14 32 ] . The second step of the insertion involves an obligatory hydrolysis of ATP that is tightly coupled with the transfer of the chelated Mg 2+to the protoporphyrin ring by BchH [ 49 ] . Although the details differ from midasin, particularly with respect to the subunit composition of the AAA ring, this chelation reaction provides a structural model suggesting that the function of the midasin M-domain may be to regulate the ATPase activity of the AAA protomers in the pseudo-hexameric ring and thus couple ATP hydrolysis to the binding of a protein ligand at the MIDAS site.
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