2pqi

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(New page: 200px<br /><applet load="2pqi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pqi, resolution 2.5&Aring;" /> '''Crystal structure of ...)
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[[Image:2pqi.jpg|left|200px]]<br /><applet load="2pqi" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pqi, resolution 2.5&Aring;" />
 
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'''Crystal structure of active ribosome inactivating protein from maize (b-32)'''<br />
 
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==Overview==
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==Crystal structure of active ribosome inactivating protein from maize (b-32)==
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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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<StructureSection load='2pqi' size='340' side='right'caption='[[2pqi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2pqi]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqi OCA], [https://pdbe.org/2pqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqi RCSB], [https://www.ebi.ac.uk/pdbsum/2pqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RIPX_MAIZE RIPX_MAIZE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pqi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pqi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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<ref>PMID:17855394</ref>
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2PQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17855394 17855394]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2pqi" style="background-color:#fffaf0;"></div>
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[[Category: Zea mays]]
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[[Category: rRNA N-glycosylase]]
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[[Category: Au, S.W.N.]]
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[[Category: Cha, S.S.]]
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[[Category: Mak, A.N.S.]]
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[[Category: Shaw, P.C.]]
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[[Category: Sze, K.H.]]
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[[Category: Wong, K.B.]]
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[[Category: Wong, Y.T.]]
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[[Category: Young, J.A.]]
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[[Category: hydrolase]]
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[[Category: maize]]
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[[Category: mod]]
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[[Category: plant defense]]
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[[Category: protein synthesis inhibitor]]
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[[Category: ribosome inactivating protein]]
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[[Category: toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:20:22 2008''
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==See Also==
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*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Zea mays]]
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[[Category: Au SWN]]
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[[Category: Cha SS]]
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[[Category: Mak ANS]]
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[[Category: Shaw PC]]
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[[Category: Sze KH]]
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[[Category: Wong KB]]
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[[Category: Wong YT]]
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[[Category: Young JA]]

Current revision

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

PDB ID 2pqi

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