Words similar to mrc-lmb
Example sentences for: mrc-lmb
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Organic phosphate compounds are the central metabolites of all biological systems [ 1 2 ] . Some are the basic building blocks of nucleic acids, some like ATP and GTP, are additionally, cellular energy stores, others like cAMP or cGMP are messengers in signal transduction, and, yet others, such as FAD, NAD, thiamine phosphates and pyridoxal phosphate are cofactors for a range of enzymes [ 1 2 ] . Protein domains belonging to a relatively small set of structural folds are known to bind or catalyze reactions that utilize these organic phosphate compounds (see SCOP database: http://scop.mrc-lmb.cam.ac.uk/scop/) [ 3 4 ] . Several of these folds trace back to some of the earliest phases of the evolution of the protein world, and participate in a wide range of disparate biological functions in extant proteins [ 4 5 ] . Some folds, such as the P-loop fold, the Rossmann fold and the Hsp70-like fold, have been well studied, and comprise mainly of dedicated nucleotide binding or hydrolyzing proteins [ 6 7 8 9 ] . Others, such as the palm-domain, which is found in adenylyl cyclases and various nucleic acid polymerases, belong to more generalized protein folds that contain representatives with diverse biochemical activities [ 4 10 11 ] . Current availability of extensive genome sequence data, allows one to identify less numerous, nevertheless biological important organic phosphate-binding domains that may have previous eluded detection.
The classical adenylyl cyclases, guanylyl cyclases and the GGDEF (diguanylate cyclase) domains share the catalytic palm domain with the family B DNA polymerases, reverse transcriptases, viral RNA dependent RNA polymerases and eukaryote-type primases [ 4 13 14 ] . The pathogenic adenylyl cyclases of several bacteria and the CyaA-like proteobacteria adenylyl cyclases are extremely divergent versions of the catalytic domain seen in the Pol-β family of nucleotidyl transferases [ 15 ] (also see SCOP database: http://scop.mrc-lmb.cam.ac.uk/scop/).
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