3FLD

Crystal structure of the trai c-terminal domain

Summary for 3FLD

• Entry DOI: 10.2210/pdb3fld/pdb
• Descriptor: Protein traI, SULFATE ION (3 entities in total)
• Functional Keywords: novel alpha/beta core domain, alternative initiation, atp- binding, conjugation, dna-binding, helicase, hydrolase, nucleotide-binding, plasmid, atp-binding
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 2
• Total formula weight: 33346.70

Authors

Guogas, L.M.,Kennedy, S.A.,Redinbo, M.R. (deposition date: 2008-12-18, release date: 2009-02-10, Last modification date: 2024-02-21)

Primary citation

Guogas, L.M.,Kennedy, S.A.,Lee, J.H.,Redinbo, M.R.
A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.
J.Mol.Biol., 386:554-568, 2009

PubMed Abstract: TraI relaxase-helicase is the central catalytic component of the multiprotein relaxosome complex responsible for conjugative DNA transfer (CDT) between bacterial cells. CDT is a primary mechanism for the lateral propagation of microbial genetic material, including the spread of antibiotic resistance genes. The 2.4-A resolution crystal structure of the C-terminal domain of the multifunctional Escherichia coli F (fertility) plasmid TraI protein is presented, and specific structural regions essential for CDT are identified. The crystal structure reveals a novel fold composed of a 28-residue N-terminal alpha-domain connected by a proline-rich loop to a compact alpha/beta-domain. Both the globular nature of the alpha/beta-domain and the presence as well as rigidity of the proline-rich loop are required for DNA transfer and single-stranded DNA binding. Taken together, these data establish the specific structural features of this noncatalytic domain that are essential to DNA conjugation.

PubMed: 19136009
DOI: 10.1016/j.jmb.2008.12.057

Experimental method

X-RAY DIFFRACTION (2.4 Å)