2ezh
From Proteopedia
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SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED AVERAGE STRUCTURE
Overview
The MuA transposase of phase Mu is a large modular protein that plays a, central role in transposition. We show that the Mu end DNA-binding domain, I beta gamma, which is responsible for binding the DNA attachment sites at, each end of the Mu genome, comprises two subdomains, I beta and I gamma, that are structurally autonomous and do not interact with each other in, the absence of DNA. The solution structure of the I gamma subdomain has, been determined by multidimensional NMR spectroscopy. The structure of I, gamma comprises a four helix bundle and, despite the absence of any, significant sequence identity, the topology of the first three helices is, very similar to that of the homeodomain family of helix-turn-helix, DNA-binding proteins. The helix-turn-helix motif of I gamma, however, differs from that of the homeodomains in so far as the loop is longer and, the second helix is shorter, reminiscent of that in the POU-specific, domain.
About this Structure
2EZH is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
Reference
Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase., Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Clore GM, J Mol Biol. 1997 Oct 17;273(1):19-25. PMID:9367742
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