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1z5f

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(New page: 200px<br /><applet load="1z5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5f" /> '''Solution Structure of the Cytotoxic RC-RNase...)
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[[Image:1z5f.gif|left|200px]]<br /><applet load="1z5f" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1z5f" />
 
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'''Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus'''<br />
 
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==Overview==
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==Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus==
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Many proteins and bioactive peptides contain an N-terminal pyroglutamate, residue (Pyr1). This residue reduces the susceptibility of the protein to, aminopeptidases and often has important functional roles. The antitumor, ribonuclease RC-RNase 3 (RNase 3) from oocytes of Rana catesbeiana, (bullfrog) is one such protein. We have produced recombinant RNase 3, containing the N-terminal Pyr1 (pRNase 3) and found it to be, indistinguishable from the native RNase 3 by mass spectrometry and a, variety of other biochemical and immunological criteria. We demonstrated, by NMR analysis that the Pyr1 of pRNase 3 forms hydrogen bonds with Lys9, and Ile96 and stabilizes the N-terminal alpha-helix in a rigid, conformation. In contrast, the N-terminal alpha-helix becomes flexible and, the pKa values of the catalytic residues His10 and His97 altered when Pyr1, formation is blocked by an extra methionine at the N terminus in the, recombinant mqRNase 3. Thus, our results provide a mechanistic explanation, on the essential role of Pyr1 in maintaining the structural integrity, especially at the N-terminal alpha-helix, and in providing the proper, environment for the ionization of His10 and His97 residues for catalysis, and cytotoxicity against HeLa cells.
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<StructureSection load='1z5f' size='340' side='right'caption='[[1z5f]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z5f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_catesbeianus Lithobates catesbeianus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z5F 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">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1z5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z5f OCA], [https://pdbe.org/1z5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z5f RCSB], [https://www.ebi.ac.uk/pdbsum/1z5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z5f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9DFY7_LITCT Q9DFY7_LITCT]
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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/z5/1z5f_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=1z5f 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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Many proteins and bioactive peptides contain an N-terminal pyroglutamate residue (Pyr1). This residue reduces the susceptibility of the protein to aminopeptidases and often has important functional roles. The antitumor ribonuclease RC-RNase 3 (RNase 3) from oocytes of Rana catesbeiana (bullfrog) is one such protein. We have produced recombinant RNase 3 containing the N-terminal Pyr1 (pRNase 3) and found it to be indistinguishable from the native RNase 3 by mass spectrometry and a variety of other biochemical and immunological criteria. We demonstrated by NMR analysis that the Pyr1 of pRNase 3 forms hydrogen bonds with Lys9 and Ile96 and stabilizes the N-terminal alpha-helix in a rigid conformation. In contrast, the N-terminal alpha-helix becomes flexible and the pKa values of the catalytic residues His10 and His97 altered when Pyr1 formation is blocked by an extra methionine at the N terminus in the recombinant mqRNase 3. Thus, our results provide a mechanistic explanation on the essential role of Pyr1 in maintaining the structural integrity, especially at the N-terminal alpha-helix, and in providing the proper environment for the ionization of His10 and His97 residues for catalysis and cytotoxicity against HeLa cells.
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==About this Structure==
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Roles of N-terminal pyroglutamate in maintaining structural integrity and pKa values of catalytic histidine residues in bullfrog ribonuclease 3.,Lou YC, Huang YC, Pan YR, Chen C, Liao YD J Mol Biol. 2006 Jan 20;355(3):409-21. Epub 2005 Nov 10. PMID:16309702<ref>PMID:16309702</ref>
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1Z5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z5F 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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Roles of N-terminal pyroglutamate in maintaining structural integrity and pKa values of catalytic histidine residues in bullfrog ribonuclease 3., Lou YC, Huang YC, Pan YR, Chen C, Liao YD, J Mol Biol. 2006 Jan 20;355(3):409-21. Epub 2005 Nov 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16309702 16309702]
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</div>
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[[Category: Rana catesbeiana]]
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<div class="pdbe-citations 1z5f" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Chen, C.]]
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[[Category: Huang, Y.C.]]
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[[Category: Liao, Y.D.]]
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[[Category: Lou, Y.C.]]
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[[Category: Pan, Y.R.]]
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[[Category: bullfrog]]
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[[Category: cytotoxicity]]
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[[Category: nmr]]
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[[Category: pyroglutamate]]
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[[Category: ribonuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:44:43 2007''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 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: Lithobates catesbeianus]]
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[[Category: Chen C]]
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[[Category: Huang YC]]
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[[Category: Liao YD]]
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[[Category: Lou YC]]
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[[Category: Pan YR]]

Current revision

Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus

PDB ID 1z5f

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