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.


1jri

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jri.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1jri.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jri| PDB=1jri | SCENE= }}
{{STRUCTURE_1jri| PDB=1jri | SCENE= }}
-
'''The Crystal Structure of an Sm-like Archaeal Protein with Two Heptamers in the Asymmetric Unit.'''
+
===The Crystal Structure of an Sm-like Archaeal Protein with Two Heptamers in the Asymmetric Unit.===
-
==Overview==
+
<!--
-
Intron splicing is a prime example of the many types of RNA processing catalyzed by small nuclear ribonucleoprotein (snRNP) complexes. Sm proteins form the cores of most snRNPs, and thus to learn principles of snRNP assembly we characterized the oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs) from Pyrobaculum aerophilum (Pae) and Methanobacterium thermautotrophicum (Mth). Ultracentrifugation shows that Mth SmAP1 is exclusively heptameric in solution, whereas Pae SmAP1 forms either disulfide-bonded 14-mers or sub-heptameric states (depending on the redox potential). By electron microscopy, we show that Pae and Mth SmAP1 polymerize into bundles of well ordered fibers that probably form by head-to-tail stacking of heptamers. The crystallographic results reported here corroborate these findings by showing heptamers and 14-mers of both Mth and Pae SmAP1 in four new crystal forms. The 1.9 A-resolution structure of Mth SmAP1 bound to uridine-5'-monophosphate (UMP) reveals conserved ligand-binding sites. The likely RNA binding site in Mth agrees with that determined for Archaeoglobus fulgidus (Afu) SmAP1. Finally, we found that both Pae and Mth SmAP1 gel-shift negatively supercoiled DNA. These results distinguish SmAPs from eukaryotic Sm proteins and suggest that SmAPs have a generic single-stranded nucleic acid-binding activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12649441}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12649441 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12649441}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Heptameric]]
[[Category: Heptameric]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:45:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:41:35 2008''

Revision as of 17:41, 1 July 2008

Image:1jri.png

Template:STRUCTURE 1jri

The Crystal Structure of an Sm-like Archaeal Protein with Two Heptamers in the Asymmetric Unit.

Template:ABSTRACT PUBMED 12649441

About this Structure

1JRI is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)., Mura C, Kozhukhovsky A, Gingery M, Phillips M, Eisenberg D, Protein Sci. 2003 Apr;12(4):832-47. PMID:12649441

Page seeded by OCA on Tue Jul 1 20:41:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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