Imaging

@article{,

title = {Nucleic acids: how high resolution structural biology help us to understand Darwinian evolution},

author = {E Westhof and D J Patel},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19482468},

isbn = {19482468},

year  = {2009},

date = {2009-01-01},

journal = {Curr Opin Struct Biol},

volume = {19},

number = {3},

pages = {235-238},

note = {1879-033X (Electronic) 

Editorial 

Introductory Journal Article},

keywords = {*Evolution, Molecular  Humans  Molecular Biology/*methods  Nucleic Acids/*chemistry/metabolism  Periodicals as Topic, Unité ARN, WESTHOF},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly},

author = { M. Bergdoll and L. D. Eltis and A. D. Cameron and P. Dumas and J. T. Bolin},

year  = {1998},

date = {1998-01-01},

journal = {Protein Sci},

volume = {7},

number = {8},

pages = {1661-70},

abstract = {The crystal structures of three proteins of diverse function and low sequence similarity were analyzed to evaluate structural and evolutionary relationships. The proteins include a bacterial bleomycin resistance protein, a bacterial extradiol dioxygenase, and human glyoxalase I. Structural comparisons, as well as phylogenetic analyses, strongly indicate that the modern family of proteins represented by these structures arose through a rich evolutionary history that includes multiple gene duplication and fusion events. These events appear to be historically shared in some cases, but parallel and historically independent in others. A significant early event is proposed to be the establishment of metal-binding in an oligomeric ancestor prior to the first gene fusion. Variations in the spatial arrangements of homologous modules are observed that are consistent with the structural principles of three-dimensional domain swapping, but in the unusual context of the formation of larger monomers from smaller dimers or tetramers. The comparisons support a general mechanism for metalloprotein evolution that exploits the symmetry of a homooligomeric protein to originate a metal binding site and relies upon the relaxation of symmetry, as enabled by gene duplication, to establish and refine specific functions.},

note = {0961-8368 

Journal Article},

keywords = {*Acetyltransferases, *Evolution, Acid, Amino, Bacterial, Burkholderia/*chemistry, Crystallography, Data, Genetic, Gov't, Homology, Human, Lactoylglutathione, Lyase/*chemistry, Models, Molecular, Non-U.S., Oxygenases/chemistry, P.H.S., Phylogeny, Protein, Proteins/*chemistry, Secondary, Sequence, structure, Support, U.S., X-Ray},

pubstate = {published},

tppubtype = {article}

}