206d: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:206d.gif|left|200px]]
{{Seed}}
[[Image:206d.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_206d|  PDB=206d  |  SCENE=  }}  
{{STRUCTURE_206d|  PDB=206d  |  SCENE=  }}  


'''BASE-PAIR OPENING AND SPERMINE BINDING-B-DNA FEATURES DISPLAYED IN THE CRYSTAL STRUCTURE OF A GAL OPERON FRAGMENT: IMPLICATIONS FOR PROTEIN-DNA RECOGNITION'''
===BASE-PAIR OPENING AND SPERMINE BINDING-B-DNA FEATURES DISPLAYED IN THE CRYSTAL STRUCTURE OF A GAL OPERON FRAGMENT: IMPLICATIONS FOR PROTEIN-DNA RECOGNITION===




==Overview==
<!--  
A sequence that is represented frequently in functionally important sites involving protein-DNA interactions is GTG/CAC, suggesting that the trimer may play a role in regulatory processes. The 2.5 A resolution structure of d(CGGTGG)/d(CCACCG), a part of the interior operator (OI, nucleotides +44 to +49) of the gal operon, co-crystallized with spermine, is described herein. The crystal packing arrangement in this structure is unprecedented in a crystal of B-DNA, revealing a close packing of columns of stacked DNA resembling a 5-stranded twisted wire cable. The final structure contains one hexamer duplex, 17 water molecules and 1.5 spermine molecules per crystallographic asymmetric unit. The hexamer exhibits base-pair opening and shearing at T.A resulting in a novel non-Watson-Crick hydrogen-bonding scheme between adenine and thymine in the GTG region. The ability of this sequence to adopt unusual conformations in its GTG region may be a critical factor conferring sequence selectivity on the binding of Gal repressor. In addition, this is the first conclusive example of a crystal structure of spermine with native B-DNA, providing insight into the mechanics of polyamine-DNA binding, as well as possible explanations for the biological action of spermine.
The line below this paragraph, {{ABSTRACT_PUBMED_7596838}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7596838 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7596838}}


==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: B-dna]]
[[Category: B-dna]]
[[Category: Double helix]]
[[Category: Double helix]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:17:58 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:28:47 2008''

Revision as of 10:28, 28 July 2008

File:206d.png

Template:STRUCTURE 206d

BASE-PAIR OPENING AND SPERMINE BINDING-B-DNA FEATURES DISPLAYED IN THE CRYSTAL STRUCTURE OF A GAL OPERON FRAGMENT: IMPLICATIONS FOR PROTEIN-DNA RECOGNITION

Template:ABSTRACT PUBMED 7596838

About this Structure

Full crystallographic information is available from OCA.

Reference

Base-pair opening and spermine binding--B-DNA features displayed in the crystal structure of a gal operon fragment: implications for protein-DNA recognition., Tari LW, Secco AS, Nucleic Acids Res. 1995 Jun 11;23(11):2065-73. PMID:7596838

Page seeded by OCA on Mon Jul 28 13:28:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=206d&oldid=700633"