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.


1evp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1evp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1evp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1evp| PDB=1evp | SCENE= }}
{{STRUCTURE_1evp| PDB=1evp | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE CHIMERICAL DECAMER D(CCACTAGTG)R(G)'''
+
===CRYSTAL STRUCTURE OF THE CHIMERICAL DECAMER D(CCACTAGTG)R(G)===
-
==Overview==
+
<!--
-
The crystal structure of the chimerical decamer d(CCACTAGTG)r(G), bearing a 3'-terminal ribo-guanidine, has been solved and refined at 1.8 A resolution (R-factor 16.6%; free R-factor 22.8%). The decamer crystallizes in the orthorhombic space group P2(1)2(1)2(1) with unit cell constants a = 23.90 A, b = 45.76 A and c = 49.27 A. The structure was solved by molecular replacement using the coordinates of the isomorphous chimera r(GCG)d(TATACGC). The final model contains one duplex and 77 water molecules per asymmetric unit. Surprisingly, all residues adopt a conformation typical for A-form nucleic acids (C3'-endo type sugar pucker) although the all-DNA analog, d(CCACTAGTGG), has been crystallized in the B-form. Comparing circular dichroism spectra of the chimera and the corresponding all-DNA sequence reveals a similar trend of the former molecule to adopt an A-like conformation in solution. The results suggest that the preference of ribonucleotides for the A-form is communicated into the 5'-direction of an oligonucleotide strand, although direct interactions of the 2'-hydroxyl group can only be discerned with nucleotides in the 3'-direction of a C3'-endo puckered ribose. These observations imply that forces like water-mediated contacts, the concerted motions of backbone torsion angles, and stacking preferences, are responsible for such long-range influences. This bi-directional structural communication originating from a ribonucleotide can be expected to contribute to the stability of the A-form within all-RNA duplexes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11058136}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11058136 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11058136}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Structural conversion]]
[[Category: Structural conversion]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:34:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:05:45 2008''

Revision as of 23:05, 30 June 2008

Image:1evp.png

Template:STRUCTURE 1evp

CRYSTAL STRUCTURE OF THE CHIMERICAL DECAMER D(CCACTAGTG)R(G)

Template:ABSTRACT PUBMED 11058136

About this Structure

Full crystallographic information is available from OCA.

Reference

B-form to A-form conversion by a 3'-terminal ribose: crystal structure of the chimera d(CCACTAGTG)r(G)., Wahl MC, Sundaralingam M, Nucleic Acids Res. 2000 Nov 1;28(21):4356-63. PMID:11058136

Page seeded by OCA on Tue Jul 1 02:05:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1evp"
Personal tools