Ml4 protein from Mesorhizobium loti has a 58% sequence identity with the Ros protein from Agrobacterium tumefaciens that contains a prokaryotic Cys 2His2 zinc finger domain. Interestingly, Ml4 is a zinc-lacking protein that does not contain the Cys2His2 motif and is able to bind the Ros DNA target sequence with high affinity. Here we report the 1H, 15N and 13C NMR assignments of the Ml4 protein DNA binding domain (residue 52-151), as an important step toward elucidating at a molecular level how this prokaryotic domain can overcome the metal requirement for proper folding and DNA-binding activity. © 2009 Springer Science+Business Media B.V.
NMR assignments of the DNA binding domain of Ml4 protein from Mesorhizobium loti
RUSSO, Luigi;BAGLIVO I;ESPOSITO, Sabrina;ISERNIA, Carla;MALGIERI, Gaetano;PEDONE, Paolo Vincenzo;FATTORUSSO, Roberto
2010
Abstract
Ml4 protein from Mesorhizobium loti has a 58% sequence identity with the Ros protein from Agrobacterium tumefaciens that contains a prokaryotic Cys 2His2 zinc finger domain. Interestingly, Ml4 is a zinc-lacking protein that does not contain the Cys2His2 motif and is able to bind the Ros DNA target sequence with high affinity. Here we report the 1H, 15N and 13C NMR assignments of the Ml4 protein DNA binding domain (residue 52-151), as an important step toward elucidating at a molecular level how this prokaryotic domain can overcome the metal requirement for proper folding and DNA-binding activity. © 2009 Springer Science+Business Media B.V.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
