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.


1auu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1auu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1auu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1auu| PDB=1auu | SCENE= }}
{{STRUCTURE_1auu| PDB=1auu | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES'''
+
===SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES===
-
==Overview==
+
<!--
-
SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9305643}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9305643 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9305643}}
==About this Structure==
==About this Structure==
-
1AUU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUU OCA].
+
1AUU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUU OCA].
==Reference==
==Reference==
Line 26: Line 30:
[[Category: Rna binding domain]]
[[Category: Rna binding domain]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:43:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:38:27 2008''

Revision as of 14:38, 30 June 2008

Template:STRUCTURE 1auu

SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES

Template:ABSTRACT PUBMED 9305643

About this Structure

1AUU is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.

Reference

From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins., Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S, EMBO J. 1997 Aug 15;16(16):5019-29. PMID:9305643

Page seeded by OCA on Mon Jun 30 17:38:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools