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.


2vby

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2vby.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vby.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vby| PDB=2vby | SCENE= }}
{{STRUCTURE_2vby| PDB=2vby | SCENE= }}
-
'''FEAST OR FAMINE REGULATORY PROTEIN (RV3291C)FROM M. TUBERCULOSIS COMPLEXED WITH L-TYROSINE'''
+
===FEAST OR FAMINE REGULATORY PROTEIN (RV3291C)FROM M. TUBERCULOSIS COMPLEXED WITH L-TYROSINE===
-
==Overview==
+
<!--
-
Rv3291c gene from Mycobacterium tuberculosis codes for a transcriptional regulator belonging to the (leucine responsive regulatory protein/regulator of asparigine synthase C gene product) Lrp/AsnC-family. We have identified a novel effector-binding site from crystal structures of the apo protein, complexes with a variety of amino acid effectors, X-ray based ligand screening and qualitative fluorescence spectroscopy experiments. The new effector site is in addition to the structural characterization of another distinct site in the protein conserved in the related AsnC-family of regulators. The structures reveal that the ligand-binding loops of two crystallographically independent subunits adopt different conformations to generate two distinct effector-binding sites. A change in the conformation of the binding site loop 100-106 in the B subunit is apparently necessary for octameric association and also allows the loop to interact with a bound ligand in the newly identified effector-binding site. There are four sites of each kind in the octamer and the protein preferentially binds to aromatic amino acids. While amino acids like Phe, Tyr and Trp exhibit binding to only one site, His exhibits binding to both sites. Binding of Phe is accompanied by a conformational change of 3.7 A in the 75-83 loop, which is advantageously positioned to control formation of higher oligomers. Taken together, the present studies suggest an elegant control mechanism for global transcription regulation involving binding of ligands to the two sites, individually or collectively.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17962306}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17962306 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17962306}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Transcription regulator]]
[[Category: Transcription regulator]]
[[Category: Tyrosine complex]]
[[Category: Tyrosine complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:33:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:52:26 2008''

Revision as of 11:52, 28 July 2008

Image:2vby.png

Template:STRUCTURE 2vby

FEAST OR FAMINE REGULATORY PROTEIN (RV3291C)FROM M. TUBERCULOSIS COMPLEXED WITH L-TYROSINE

Template:ABSTRACT PUBMED 17962306

About this Structure

2VBY is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv., Shrivastava T, Ramachandran R, Nucleic Acids Res. 2007;35(21):7324-35. Epub 2007 Oct 25. PMID:17962306

Page seeded by OCA on Mon Jul 28 14:52:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vby"
Personal tools