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.


1ts9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ts9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ts9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ts9| PDB=1ts9 | SCENE= }}
{{STRUCTURE_1ts9| PDB=1ts9 | SCENE= }}
-
'''Crystal Structure of the Archaeal Homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus'''
+
===Crystal Structure of the Archaeal Homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus===
-
==Overview==
+
<!--
-
The crystal structure of ribonuclease P protein aRpp29 from the sulfate-reducing hyperthermophile Archaeoglobus fulgidus was determined at 1.7 A resolution using X-ray diffraction methods. The central feature of this archaeal protein is a sheet of six antiparallel beta-strands twisted around a conserved hydrophobic core. Residues near the N- and C-termini form helical structures that are oriented in an antiparallel manner. A comparison of conserved amino acids indicates that archaeal aRpp29 is homologous to human ribonuclease P protein Rpp29. The aRpp29 protein is structurally similar to bacterial transcription factors Hfq and NusG, as well as the Sm and Sm-like RNA-associated proteins from eukarya. The crystal structure of A. fulgidus aRpp29 differs from the previously reported solution structure, where NMR data did not detect the helices and indicated that approximately 40% of the residues are relatively flexible or disordered. Circular dichroism data indicate that the protein has less helical content than the amount observed in the crystal, suggesting that in solution the helical regions are unfolded or in equilibrium between folded and unfolded forms; this hypothesis is consistent with amide proton exchange rate data. Surface residues that are conserved from archaea to humans and are likely to interact with the ribonuclease P RNA or other protein subunits are identified in the structure. The model of the aRpp29 protein defined by this work provides an essential step toward eventually understanding the overall architecture of ribonuclease P.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15518563}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15518563 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15518563}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Selenomethionine]]
[[Category: Selenomethionine]]
[[Category: Sm-fold]]
[[Category: Sm-fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:18:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:29:37 2008''

Revision as of 03:29, 29 July 2008

Image:1ts9.png

Template:STRUCTURE 1ts9

Crystal Structure of the Archaeal Homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus

Template:ABSTRACT PUBMED 15518563

About this Structure

1TS9 is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus., Sidote DJ, Heideker J, Hoffman DW, Biochemistry. 2004 Nov 9;43(44):14128-38. PMID:15518563

Page seeded by OCA on Tue Jul 29 06:29:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ts9"
Personal tools