2ivm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2ivm.jpg|left|200px]]
{{Seed}}
[[Image:2ivm.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ivm|  PDB=2ivm  |  SCENE=  }}  
{{STRUCTURE_2ivm|  PDB=2ivm  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A TRANSCRIPTIONAL REGULATOR'''
===CRYSTAL STRUCTURE OF A TRANSCRIPTIONAL REGULATOR===




==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 26: Line 30:
[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Transcriptional regulator]]
[[Category: Transcriptional regulator]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:56:35 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:29:37 2008''

Revision as of 13:29, 29 July 2008

File:2ivm.png

Template:STRUCTURE 2ivm

CRYSTAL STRUCTURE OF A TRANSCRIPTIONAL REGULATOR

Template:ABSTRACT PUBMED 17962306

About this Structure

2IVM 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 Tue Jul 29 16:29:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2ivm&oldid=749058"