1z5f: Difference between revisions
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'''Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus''' | {{Structure | ||
|PDB= 1z5f |SIZE=350|CAPTION= <scene name='initialview01'>1z5f</scene> | |||
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'''Solution Structure of the Cytotoxic RC-RNase 3 with a Pyroglutamate Residue at the N-terminus''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Z5F is a [ | 1Z5F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5F OCA]. | ||
==Reference== | ==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:[http:// | 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://www.ncbi.nlm.nih.gov/pubmed/16309702 16309702] | ||
[[Category: Rana catesbeiana]] | [[Category: Rana catesbeiana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
''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 15:31:23 2008'' | ||
Revision as of 13:31, 20 March 2008
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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
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