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1rl0
From Proteopedia
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| - | [[Image:1rl0.gif|left|200px]] | + | [[Image:1rl0.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of a new ribosome-inactivating protein (RIP): dianthin 30''' | + | {{Structure |
| + | |PDB= 1rl0 |SIZE=350|CAPTION= <scene name='initialview01'>1rl0</scene>, resolution 1.40Å | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of a new ribosome-inactivating protein (RIP): dianthin 30''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RL0 is a [ | + | 1RL0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dianthus_caryophyllus Dianthus caryophyllus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RL0 OCA]. |
==Reference== | ==Reference== | ||
| - | The 1.4 anstroms structure of dianthin 30 indicates a role of surface potential at the active site of type 1 ribosome inactivating proteins., Fermani S, Falini G, Ripamonti A, Polito L, Stirpe F, Bolognesi A, J Struct Biol. 2005 Feb;149(2):204-12. PMID:[http:// | + | The 1.4 anstroms structure of dianthin 30 indicates a role of surface potential at the active site of type 1 ribosome inactivating proteins., Fermani S, Falini G, Ripamonti A, Polito L, Stirpe F, Bolognesi A, J Struct Biol. 2005 Feb;149(2):204-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15681236 15681236] |
[[Category: Dianthus caryophyllus]] | [[Category: Dianthus caryophyllus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Ripamonti, A.]] | [[Category: Ripamonti, A.]] | ||
[[Category: Stirpe, F.]] | [[Category: Stirpe, F.]] | ||
| - | [[Category: alpha and beta | + | [[Category: alpha and beta region]] |
[[Category: mixed beta-sheet]] | [[Category: mixed beta-sheet]] | ||
| - | ''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 13:53:02 2008'' |
Revision as of 11:53, 20 March 2008
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| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a new ribosome-inactivating protein (RIP): dianthin 30
Overview
Ribosome inactivating proteins (RIPs) are plant proteins with enzymatic activity identified as rRNA N-glycosidase (EC 3.2.2.22), which cleaves the N-glycosidic bond of a specific adenine on the ricin/sarcin region of rRNA, thus causing inhibition of protein synthesis. They also depurinate extensively DNA and other polynucleotides. The three-dimensional structure of dianthin 30, a type 1 (single-chain) RIP of Dianthus caryophyllus (leaves), is now described at 1.4 angstroms, a resolution never achieved before for any RIP. The fold typical of RIPs is conserved, despite some differences in the loop regions. The general structure comparison by superimposed alpha-carbon (249 atoms) and the sequence alignment by structure for dianthin 30 and saporin-S6 give a root mean square deviation of 0.625 angstroms. Despite the differences reported for the biological activities of the two RIPs, their structures fit quite well and both show a protein segment containing strands beta7, beta8, and beta9 shorter than other RIPs. However, the surface electrostatic potential in the active site region neatly distinguishes dianthin 30 from saporin-S6. The possible relationship between the charge distribution and the behavior of the proteins toward different substrates is discussed.
About this Structure
1RL0 is a Single protein structure of sequence from Dianthus caryophyllus. Full crystallographic information is available from OCA.
Reference
The 1.4 anstroms structure of dianthin 30 indicates a role of surface potential at the active site of type 1 ribosome inactivating proteins., Fermani S, Falini G, Ripamonti A, Polito L, Stirpe F, Bolognesi A, J Struct Biol. 2005 Feb;149(2):204-12. PMID:15681236
Page seeded by OCA on Thu Mar 20 13:53:02 2008
