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.


1v76

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1v76.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1v76.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1v76| PDB=1v76 | SCENE= }}
{{STRUCTURE_1v76| PDB=1v76 | SCENE= }}
-
'''Crystal Structure of Archaeal Ribonuclease P Protein Ph1771p from Pyrococcus horikoshii OT3'''
+
===Crystal Structure of Archaeal Ribonuclease P Protein Ph1771p from Pyrococcus horikoshii OT3===
-
==Overview==
+
<!--
-
Ribonuclease P (RNase P) is the endonuclease responsible for the removal of 5' leader sequences from tRNA precursors. The crystal structure of an archaeal RNase P protein, Ph1771p (residues 36-127) from hyperthermophilic archaeon Pyrococcus horikoshii OT3 was determined at 2.0 A resolution by X-ray crystallography. The structure is composed of four helices (alpha1-alpha4) and a six-stranded antiparallel beta-sheet (beta1-beta6) with a protruding beta-strand (beta7) at the C-terminal region. The strand beta7 forms an antiparallel beta-sheet by interacting with strand beta4 in a symmetry-related molecule, suggesting that strands beta4 and beta7 could be involved in protein-protein interactions with other RNase P proteins. Structural comparison showed that the beta-barrel structure of Ph1771p has a topological resemblance to those of Staphylococcus aureus translational regulator Hfq and Haloarcula marismortui ribosomal protein L21E, suggesting that these RNA binding proteins have a common ancestor and then diverged to specifically bind to their cognate RNAs. The structure analysis as well as structural comparison suggested two possible RNA binding sites in Ph1771p, one being a concave surface formed by terminal alpha-helices (alpha1-alpha4) and beta-strand beta6, where positively charged residues are clustered. A second possible RNA binding site is at a loop region connecting strands beta2 and beta3, where conserved hydrophilic residues are exposed to the solvent and interact specifically with sulfate ion. These two potential sites for RNA binding are located in close proximity. The crystal structure of Ph1771p provides insight into the structure and function relationships of archaeal and eukaryotic RNase P.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15317976}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15317976 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15317976}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Archaeal rnase p protein]]
[[Category: Archaeal rnase p protein]]
[[Category: Rna binding protein]]
[[Category: Rna binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:10:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:22:42 2008''

Revision as of 17:22, 27 July 2008

Image:1v76.png

Template:STRUCTURE 1v76

Crystal Structure of Archaeal Ribonuclease P Protein Ph1771p from Pyrococcus horikoshii OT3

Template:ABSTRACT PUBMED 15317976

About this Structure

1V76 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29., Numata T, Ishimatsu I, Kakuta Y, Tanaka I, Kimura M, RNA. 2004 Sep;10(9):1423-32. PMID:15317976

Page seeded by OCA on Sun Jul 27 20:22:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v76"
Personal tools