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How does the structure of E. coli DNA Polymerase III relate to its function?

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Have a little read: ... How does the structure of E. coli DNA Polymerase III relate to its function? DNA polymerase III is an asymmetrical dimer (that is, it lacks inherent symmetry) one half of which is devoted to synthesizing the leading strand at the advancing replication fork and the other, the lagging strand. It is composed of 18 subunits in total (only ten of which we shall go on to discuss as their functions are understood), from only ten structural genes. Thus, more than one subunit is produced from one gene - for example, subunit tau and gamma are produced from the same gene, indeed they are both motor ATPases. The sequence of events is as follows * The ß dimer and the clamp loading complex bind to template DNA to form what is known as a pre-initiation complex * This pre-initiation complex then binds with high affinity to DNA polymerase III core enzyme (?, ? and ?),

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