3fld is a 2 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
A Novel Fold in the TraI Relaxase-Helicase C-Terminal Domain Is Essential for Conjugative DNA Transfer.,Guogas LM, Kennedy SA, Lee JH, Redinbo MR J Mol Biol. 2009 Feb 20;386(2):554-68. Epub 2008 Dec 30. PMID:19136009[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Guogas LM, Kennedy SA, Lee JH, Redinbo MR. A Novel Fold in the TraI Relaxase-Helicase C-Terminal Domain Is Essential for Conjugative DNA Transfer. J Mol Biol. 2009 Feb 20;386(2):554-68. Epub 2008 Dec 30. PMID:19136009 doi:S0022-2836(08)01579-9
