2ezi
From Proteopedia
SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, 30 STRUCTURES
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
2EZI 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 Page seeded by OCA on Sun May 4 03:17:20 2008
