Sandbox reserved 330: Difference between revisions
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Previous studies of toxin families include MazF, ChpAK, and PemK, which all code for endoribonuclease that activates cellular mRNAs by cleaving them at specific sites. Recently, there is a Bacillus subtilis gene product discovered, EndoA, that is a member of RNAses, which is likely the gene product of the YdcE gene. This EndoA has similar cleavage pattern specificity as MazF and PemK, with cleavage products of a 3’phosphate and 5’OH group<ref name="Pellegrini"/>. Further study revealed that a coexpression of an upstream gene, YdcD reverses the effects of this particular toxin, and thus, this is the first antitoxin-toxin system of Bacillus subtilis. | Previous studies of toxin families include MazF, ChpAK, and PemK, which all code for endoribonuclease that activates cellular mRNAs by cleaving them at specific sites. Recently, there is a Bacillus subtilis gene product discovered, EndoA, that is a member of RNAses, which is likely the gene product of the YdcE gene. This EndoA has similar cleavage pattern specificity as MazF and PemK, with cleavage products of a 3’phosphate and 5’OH group<ref name="Pellegrini"/>. Further study revealed that a coexpression of an upstream gene, YdcD reverses the effects of this particular toxin, and thus, this is the first antitoxin-toxin system of Bacillus subtilis. | ||
==Structure== | ==Structure== | ||
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Complexes of YdcE reveal that the two active sites of the enzyme are located peripherally at the dimer interface, and are shown to be composed of residues contributed from both monomers of the dimer. The two active sites of the native YdcE protein structure have a few differences to those when complexed with other proteins, however, the largest difference is in the repositioning of the aromatic ring of the Phe8, which is rotated approximately by 32° in the complex structure relative to the native YdcE protein<ref name="Almrud"/>. | Complexes of YdcE reveal that the two active sites of the enzyme are located peripherally at the dimer interface, and are shown to be composed of residues contributed from both monomers of the dimer. The two active sites of the native YdcE protein structure have a few differences to those when complexed with other proteins, however, the largest difference is in the repositioning of the aromatic ring of the Phe8, which is rotated approximately by 32° in the complex structure relative to the native YdcE protein<ref name="Almrud"/>. | ||
The active site of the YdcE protein is composed of residues from both monomers, with key active site residues consisting of Pro1, Arg 11, Arg 38, Phe50. Dimerization of the two monomers include Pro1, which is presumed to be the catalytic base and is from one subunit, while Phe8, Arg 10, Trp 51, and Tyr72 are from the other monomer<ref name="Almrud"/>. | The active site of the YdcE protein is composed of residues from both monomers, with key active site residues consisting of Pro1, Arg 11, Arg 38, Phe50. Dimerization of the two monomers include Pro1, which is presumed to be the catalytic base and is from one subunit, while Phe8, Arg 10, Trp 51, and Tyr72 are from the other monomer<ref name="Almrud"> Almrud, J.J., Kern, A.D., Wang, S.C., Czerwinski, R.M., Johnson, W.H., Murzin, A.G., Hackert, M.L., Whitman, C.P. The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli., confirms the structural basis for oligomer diversity. Biochemistry.2002. August;41(40):12010-12024</ref>. | ||
<references/> | <references/> | ||
