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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.
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.
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.
In most AAA proteins, the ring structure is formed by six identical polypeptide subunits, with each contributing a single AAA protomer [ 14 ] . However, the AAA motor dynein differs in having six distinct AAA protomers disposed in tandem on a single polypeptide subunit of unusually high molecular weight, and it is believed to form a unimolecular pseudo-hexameric AAA ring [ 5 6 16 ] .
The AAA domain of midasin, like that of dynein, contains six tandem copies of the amino acid sequence motifs that characterize AAA protomers (Fig.
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