2pqi
From Proteopedia
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| - | [[Image:2pqi.jpg|left|200px]] | + | [[Image:2pqi.jpg|left|200px]] |
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| - | '''Crystal structure of active ribosome inactivating protein from maize (b-32)''' | + | {{Structure |
| + | |PDB= 2pqi |SIZE=350|CAPTION= <scene name='initialview01'>2pqi</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] | ||
| + | |GENE= b-32, CRIP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 Zea mays]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of active ribosome inactivating protein from maize (b-32)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PQI is a [ | + | 2PQI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQI OCA]. |
==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:// | + | 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] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:12 2008'' |
Revision as of 16:16, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | b-32, CRIP3 (Zea mays) | ||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of active ribosome inactivating protein from maize (b-32)
Overview
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.
About this Structure
2PQI is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
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:17855394
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