1qbj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA, binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1, angstrom crystal structure of Zalpha complexed to DNA reveals that the, substrate is in the left-handed Z conformation. The contacts between, Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate, backbone, which provides a basis for the specificity for the Z, conformation. A single base contact is observed to guanine in the syn, conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix, motif, frequently used to recognize B-DNA, is used by Zalpha to contact, Z-DNA.
+
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA.
==Disease==
==Disease==
Line 17: Line 17:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Rich, A.]]
[[Category: Rich, A.]]
-
[[Category: Rould, M.A.]]
+
[[Category: Rould, M A.]]
[[Category: Schwartz, T.]]
[[Category: Schwartz, T.]]
[[Category: protein/z-dna complex]]
[[Category: protein/z-dna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:43:49 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:54 2008''

Revision as of 12:38, 21 February 2008


1qbj, resolution 2.1Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE ZALPHA Z-DNA COMPLEX

Contents

Overview

The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA.

Disease

Known diseases associated with this structure: Dyschromatosis symmetrica hereditaria OMIM:[601059]

About this Structure

1QBJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA., Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A, Science. 1999 Jun 11;284(5421):1841-5. PMID:10364558

Page seeded by OCA on Thu Feb 21 14:37:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools