2L7Q
Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155
Summary for 2L7Q
| Entry DOI | 10.2210/pdb2l7q/pdb |
| NMR Information | BMRB: 17370 |
| Descriptor | Conserved protein found in conjugate transposon (1 entity in total) |
| Functional Keywords | nesg, structural genomics, psi-biology, protein structure initiative, northeast structural genomics consortium, unknown function |
| Biological source | Bacteroides vulgatus |
| Total number of polymer chains | 1 |
| Total formula weight | 14662.17 |
| Authors | Yang, Y.,Ramelot, T.A.,Cort, J.R.,Wang, D.,Ciccosanti, C.,Janjua, H.,Acton, T.B.,Xiao, R.,Everett, J.K.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2010-12-20, release date: 2010-12-29, Last modification date: 2024-05-15) |
| Primary citation | Ramelot, T.A.,Yang, Y.,Xiao, R.,Acton, T.B.,Everett, J.K.,Montelione, G.T.,Kennedy, M.A. Solution NMR structure of BT_0084, a conjugative transposon lipoprotein from Bacteroides thetaiotamicron. Proteins, 80:667-670, 2012 Cited by PubMed Abstract: Here we describe the solution NMR structure of the 120 amino acid fragment of BT_0084, without the N-terminal lipoprotein targeting sequence, encoded in a conjugative transposon (CTn) in the genome of Bacteroides thetaiotamicron. BT_0084 belongs to a conserved family of TraQ lipoproteins that are encoded at the end of the tra operon, which contains genes essential for transfer of CTns. The structure belongs to the immunoglobulin superfamily and shares structural similarity, albeit low sequence identity (< 15%), to other proteins involved in pili production for bacterial cell attachment. Although its role in repression of CTn transfer remains to be determined, the structure of BT_0084 reported here represents the first from the Bacteroides TraQ family and should facilitate further understanding of the tra operon-regulated transfer of CTns. PubMed: 22116783DOI: 10.1002/prot.23235 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report






