2ezi
SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, 30 STRUCTURES
OverviewOverview
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 StructureAbout this Structure
2EZI is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
ReferenceReference
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