1b28: Difference between revisions

Revision as of 18:04, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1b28.png

Template:STRUCTURE 1b28

ARC REPRESSOR MYL MUTANT FROM SALMONELLA BACTERIOPHAGE P22ARC REPRESSOR MYL MUTANT FROM SALMONELLA BACTERIOPHAGE P22

Template:ABSTRACT PUBMED 10320329

About this StructureAbout this Structure

1B28 is a Single protein structure of sequence from Enterobacteria phage p22. Full experimental information is available from OCA.

ReferenceReference

The solution structure and dynamics of an Arc repressor mutant reveal premelting conformational changes related to DNA binding., Nooren IM, Rietveld AW, Melacini G, Sauer RT, Kaptein R, Boelens R, Biochemistry. 1999 May 11;38(19):6035-42. PMID:10320329

Page seeded by OCA on Mon Jun 30 18:04:22 2008

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-[[Image:1b28.gif|left|200px]]
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 {{STRUCTURE_1b28|  PDB=1b28  |  SCENE=  }}
-'''ARC REPRESSOR MYL MUTANT FROM SALMONELLA BACTERIOPHAGE P22'''
+===ARC REPRESSOR MYL MUTANT FROM SALMONELLA BACTERIOPHAGE P22===
-==Overview==
+<!--
-The solution structure of the hyperstable MYL mutant (R31M/E36Y/R40L) of the Arc repressor of bacteriophage P22 was determined by NMR spectroscopy and compared to that of the wild-type Arc repressor. A backbone rmsd versus the average of 0.37 A was obtained for the well-defined core region. For both Arc-MYL and the wild-type Arc repressor, evidence for a fast equilibrium between a packed ("in") conformation and an extended ("out") conformation of the side chain of Phe 10 was found. In the MYL mutant, the "out" conformation is more highly populated than in the wild-type Arc repressor. The Phe 10 is situated in the DNA-binding beta-sheet of the Arc dimer. While its "in" conformation appears to be the most stable, the "out" conformation is known to be present in the operator-bound form of Arc, where the Phe 10 ring contacts the phosphate backbone [Raumann, B. E., et al. (1994) Nature 367, 754-757]. As well as DNA binding, denaturation by urea and high temperatures induces the functionally active "out" conformation. With a repacking of the hydrophobic core, this characterizes a premelting transition of the Arc repressor. The dynamical properties of the Arc-MYL and the wild-type Arc repressor were further characterized by 15N relaxation and hydrogen-deuterium exchange experiments. The increased main chain mobility at the DNA binding site compared to that of the core of the protein as well as the reorientation of the side chain of Phe 10 is suggested to play an important role in specific DNA binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_10320329}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10320329 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10320329}}
 ==About this Structure==
-B28 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B28 OCA].
+B28 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B28 OCA].
 ==Reference==
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 [[Category: Hyperstable mutant]]
 [[Category: Transcription regulation]]
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