2pqi: Difference between revisions

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[[Image:2pqi.jpg|left|200px]]
{{Seed}}
[[Image:2pqi.png|left|200px]]


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{{STRUCTURE_2pqi|  PDB=2pqi  |  SCENE=  }}  
{{STRUCTURE_2pqi|  PDB=2pqi  |  SCENE=  }}  


'''Crystal structure of active ribosome inactivating protein from maize (b-32)'''
===Crystal structure of active ribosome inactivating protein from maize (b-32)===




==Overview==
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Maize ribosome-inactivating protein is classified as a class III or an atypical RNA N-glycosidase. It is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form. As the first structural example of this class of proteins, crystals of the precursor and the active form were diffracted to 2.4 and 2.5 A, respectively. The two proteins are similar, with main chain root mean square deviation (RMSD) of 0.519. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake. Like bacterial ribosome-inactivating proteins, maize ribosome-inactivating protein does not have a back-up glutamate in the active site, which helps the protein to retain some activity if the catalytic glutamate is mutated. The structure reveals that the active site is too small to accommodate two glutamate residues. Our structure suggests that maize ribosome-inactivating protein may represent an intermediate product in the evolution of ribosome-inactivating proteins.
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{{ABSTRACT_PUBMED_17855394}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site., Mak AN, Wong YT, An YJ, Cha SS, Sze KH, Au SW, Wong KB, Shaw PC, Nucleic Acids Res. 2007;35(18):6259-67. Epub 2007 Sep 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17855394 17855394]
Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site., Mak AN, Wong YT, An YJ, Cha SS, Sze KH, Au SW, Wong KB, Shaw PC, Nucleic Acids Res. 2007;35(18):6259-67. Epub 2007 Sep 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17855394 17855394]
Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment., Walsh TA, Morgan AE, Hey TD, J Biol Chem. 1991 Dec 5;266(34):23422-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1744135 1744135]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Zea mays]]
[[Category: Zea mays]]
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[[Category: Ribosome inactivating protein]]
[[Category: Ribosome inactivating protein]]
[[Category: Toxin]]
[[Category: Toxin]]
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