This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1z5f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1z5f |SIZE=350|CAPTION= <scene name='initialview01'>1z5f</scene>
|PDB= 1z5f |SIZE=350|CAPTION= <scene name='initialview01'>1z5f</scene>
|SITE=
|SITE=
-
|LIGAND=
+
|LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1kvz|1KVZ]]
 +
|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>
}}
}}
Line 33: Line 36:
[[Category: ribonuclease]]
[[Category: ribonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:31:23 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:29:18 2008''

Revision as of 22:29, 30 March 2008

Image:1z5f.gif


PDB ID 1z5f

Drag the structure with the mouse to rotate
Ligands:
Related: 1KVZ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 Mon Mar 31 01:29:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z5f"
Personal tools