2EZI

SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, 30 STRUCTURES

Summary for 2EZI

• Entry DOI: 10.2210/pdb2ezi/pdb
• Descriptor: TRANSPOSASE (1 entity in total)
• Functional Keywords: dna-binding protein, transposition, dna binding protein
• Biological source: Enterobacteria phage Mu
• Total number of polymer chains: 1
• Total formula weight: 8880.12

Authors

Clore, G.M.,Clubb, R.T.,Schumaker, S.,Gronenborn, A.M. (deposition date: 1997-07-25, release date: 1997-12-03, Last modification date: 2024-05-29)

Primary citation

Clubb, R.T.,Schumacher, S.,Mizuuchi, K.,Gronenborn, A.M.,Clore, G.M.
Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase.
J.Mol.Biol., 273:19-25, 1997

PubMed Abstract: 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.

PubMed: 9367742
DOI: 10.1006/jmbi.1997.1312

Experimental method

SOLUTION NMR