Words similar to midas
Example sentences for: midas
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One possibility is that the MIDAS site serves to attach protein ligands through a mechanism involving participation of a glutamate or aspartate residue on the ligand in the coordination of a Mg 2+ion at the MIDAS site of midasin, in a manner similar to that by which the MIDAS site in integrin I-domains appears to mediate attachment of collagen through the glutamate in the GFOGER binding motif [ 36 ] . Interestingly, the related RGE ligand-binding motif [ 41 ] occurs in a conserved region of the midasin AAA-domain (yeast, residues 1835-1838), as well as in the AAA-domain of Mg chelatases [ 32 ] . The presence of this consensus binding motif in the AAA domain raises the possibility of the midasin molecule folding back onto itself, with the M-domain becoming attached to one face of the AAA domain and perhaps regulating access to its central chamber, in a manner analogous to that in which the 19S proteasome regulator, also an AAA protein, controls access to the central proteolytic chamber of the proteasome [ 42 ] .
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 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.
The domain contains a full set of MIDAS sequence motifs consisting of hhhhDxSxS, followed after ~70 residues by a conserved threonine, followed after a further ~30 residues by hhhh[S,T]DG, where h is any hydrophobic residue and x is any residue (Fig.
The second is the highly conserved sequence RKDKIWLRRTKPSKRQ (residues 4687-4702) located in the NH 2 -extension of the M-domain, immediately upstream from the first MIDAS motif.
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