1z5f

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[[Image:1z5f.gif|left|200px]]
[[Image:1z5f.gif|left|200px]]
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{{Structure
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|PDB= 1z5f |SIZE=350|CAPTION= <scene name='initialview01'>1z5f</scene>
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The line below this paragraph, containing "STRUCTURE_1z5f", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>
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{{STRUCTURE_1z5f| PDB=1z5f | SCENE= }}
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|RELATEDENTRY=[[1kvz|1KVZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z5f OCA], [http://www.ebi.ac.uk/pdbsum/1z5f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z5f RCSB]</span>
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'''Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus'''
'''Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus'''
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[[Category: Lou, Y C.]]
[[Category: Lou, Y C.]]
[[Category: Pan, Y R.]]
[[Category: Pan, Y R.]]
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[[Category: bullfrog]]
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[[Category: Bullfrog]]
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[[Category: cytotoxicity]]
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[[Category: Cytotoxicity]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: pyroglutamate]]
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[[Category: Pyroglutamate]]
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[[Category: ribonuclease]]
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[[Category: Ribonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:11:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:29:18 2008''
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Revision as of 14:11, 3 May 2008

Image:1z5f.gif

Template:STRUCTURE 1z5f

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


Overview

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.

About this Structure

1Z5F is a Single protein structure of sequence from Rana catesbeiana. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 17:11:51 2008

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