A model for the RecA protein of Mycoplasma synoviae
Genet. mol. biol
; 30(1,suppl): 290-295, 2007. tab, ilus
Article
in English
| LILACS
| ID: lil-450447
Responsible library:
BR1.1
ABSTRACT
In this work, we predict a structural model for the RecA protein from M. synoviae (MsRecA) by theoretical homology modeling and evaluate the occurrence of polymorphisms in this protein within several isolates of this species. The structural model suggested for MsRecA conserves the main domains present in MtRecA and EcRecA. The L1 and L2 regions showed six and three amino acid substitutions, respectively, which apparently do not affect the conformation and function of MsRecA. The C-terminal domain is shorter than that found in EcRecA and MtRecA, which may increase its capacity to bind dsDNA and displace SSB, compensating the absence of recombination initiation enzymes. The MS59 isolate RecA sequence showed one polymorphism which does not affect its functions since these belong to the same physical-chemical group.
Full text:
Available
Collection:
International databases
Database:
LILACS
Type of study:
Prognostic study
Language:
English
Journal:
Genet. mol. biol
Journal subject:
Genetics
Year:
2007
Document type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Laboratório Nacional de Computação Científica/BR
/
Universidade Federal do Rio Grande do Norte/BR