Atomic-resolution structure of the cellulose synthase regulator cyclic diguanylic acid.
AUTOR(ES)
Egli, M
RESUMO
Cyclic diguanylic acid acts as a regulator for cellulose synthase activity in the bacterium Acetobacter xylinum. We report the x-ray crystal structure of the regulator at atomic resolution. The structure contains two independent molecules that adopt almost identical conformations. The two molecules form self-intercalated units that are stacked on each other. Two different G.G base-pairing modes occur between the stacks. The more stable one has two or possibly three hydrogen bonds between two guanines and is related to the type of hydrogen bonding that is believed to exist between G-rich strands at the ends of chromosomes.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=53870Documentos Relacionados
- An atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl–CoA synthase
- Evidence for a cyclic diguanylic acid-dependent cellulose synthase in plants.
- Cyclic diguanylic acid and cellulose synthesis in Agrobacterium tumefaciens.
- Polypeptide composition of bacterial cyclic diguanylic acid-dependent cellulose synthase and the occurrence of immunologically crossreacting proteins in higher plants.
- The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid.