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Example sentences for: protomers
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Concomitant with this development of asymmetrical structure, the AAA1 protomer of the dynein motor unit evolved a functional dominance, in which it alone retains the full ability for binding and hydrolysis of ATP, while AAA2, AAA3 and AAA4 have lost the capability for hydrolysis and the most degenerate protomers AAA5 and AAA6 show no significant binding of ATP [ 20 21 22 ] . In midasin, the specialization of AAA protomers appears to have taken a less drastic course than in dynein.
3; see also reference [ 5 ] ). The Walker A motif GxxxxGK [T,S] and Walker B motif hhhhDExx (where h is any hydrophobic residue and x is any residue), that contain residues essential for ATP binding and hydrolysis in all P-type ATPases [ 17 ] , are present in their canonical forms in the AAA2, AAA3, AAA4, and AAA5 protomers of midasin for all the organisms in Figure 3. The Walker A motif is present also in AAA1 and AAA6, although the Walker B motif in these protomers is deviant.
There is no indication that any of these joining polypeptides contains a ATP-sensitive microtubule-binding site resembling that located between the AAA4 and AAA5 protomers of dynein [ 46 ] . The position of the N-terminal domain of midasin relative to the AAA domain is similar to that of the stem domain of dynein, and in several organisms the midasin N-terminal domain contains a cluster of basic residues that has the potential to bind microtubules in an ATP-insensitive manner.
The AAA domain has been affected relatively little: all six AAA protomers are retained and the overall length of the domain is reduced by only ~19%.
The essentially complete retention of the M-domain and the hexameric assembly of protomers in the AAA domain emphasizes the critical importance of these domains to the proper functioning of midasin.
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