2JVW

Solution NMR structure of uncharacterized protein Q5E7H1 from Vibrio fischeri. Northeast Structural Genomics target VfR117

Summary for 2JVW

• Entry DOI: 10.2210/pdb2jvw/pdb
• NMR Information: BMRB: 15491
• Descriptor: Uncharacterized protein (1 entity in total)
• Functional Keywords: solution nmr structure, alpha helical protein, structural genomics, unknown function, psi-2, protein structure initiative, northeast structural genomics consortium, nesg
• Biological source: Vibrio fischeri
• Total number of polymer chains: 1
• Total formula weight: 10746.40

Authors

Aramini, J.M.,Rossi, P.,Wang, D.,Nwosu, C.,Owens, L.A.,Xiao, R.,Liu, J.,Baran, M.C.,Swapna, G.V.T.,Acton, T.B.,Rost, B.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2007-09-26, release date: 2007-10-16, Last modification date: 2024-05-08)

Primary citation

Aramini, J.M.,Rossi, P.,Fischer, M.,Xiao, R.,Acton, T.B.,Montelione, G.T.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins, 79:2988-2991, 2011

PubMed Abstract: Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri, the first structural representative from this protein domain family. We demonstrate that the structure of VF0530 adopts a unique four-helix motif that shows some similarity to the C-terminal double-stranded DNA (dsDNA) binding domain of RecA, as well as other nucleic acid binding domains. Moreover, gel shift binding data indicate a potential dsDNA binding role for VF0530.

PubMed: 21905121
DOI: 10.1002/prot.23121

Experimental method

SOLUTION NMR