1k8g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1k8g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k8g, resolution 2.6&Aring;" /> '''Crystal Structure of ...)
Line 1: Line 1:
-
[[Image:1k8g.gif|left|200px]]<br /><applet load="1k8g" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1k8g.gif|left|200px]]<br /><applet load="1k8g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k8g, resolution 2.6&Aring;" />
caption="1k8g, resolution 2.6&Aring;" />
'''Crystal Structure of the N-terminal domain of Oxytricha nova telomere end binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA'''<br />
'''Crystal Structure of the N-terminal domain of Oxytricha nova telomere end binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA'''<br />
==Overview==
==Overview==
-
Oxytricha nova telomere end-binding protein specifically recognizes and, caps single strand (T(4)G(4))(n) telomeric DNA at the very 3'-ends of O., nova macronuclear chromosomes. Proteins homologous to the N-terminal, domain of OnTEBP alpha subunit have now been identified in Oxytricha, trifallax, Stylonychia mytilis, Euplotes crassus, Schizosaccharomyces, pombe, and Homo sapiens, suggesting that this protein is widely, distributed in eukaryotes. We describe here the crystal structures of the, N-terminal single-stranded DNA (ssDNA)-binding domain of O. nova telomere, end-binding protein alpha subunit both uncomplexed and complexed with, single strand telomeric DNA. These structures show how the N-terminal, domain of alpha alone, in the absence of the beta subunit and without, alpha dimerization, can bind single-stranded telomeric DNA in a, sequence-specific and 3'-end-specific manner. Furthermore, comparison of, the uncomplexed and complexed forms of this protein shows that the, ssDNA-binding site is largely pre-organized in the absence of ssDNA with, modest, but interesting, rearrangements of amino acid side-chains that, compose the ssDNA-binding site. The structures described here extend our, understanding of structures of O. nova telomeric complexes by adding, uncomplexed and complexed forms of monomeric alpha to previously described, structures for (alpha 56/ssDNA)(2) dimer and alpha 56/beta 28/ssDNA, ternary complexes. We believe that each of these four structures represent, intermediates in an ordered assembly/disassembly pathway for O. nova, telomeric complexes.
+
Oxytricha nova telomere end-binding protein specifically recognizes and caps single strand (T(4)G(4))(n) telomeric DNA at the very 3'-ends of O. nova macronuclear chromosomes. Proteins homologous to the N-terminal domain of OnTEBP alpha subunit have now been identified in Oxytricha trifallax, Stylonychia mytilis, Euplotes crassus, Schizosaccharomyces pombe, and Homo sapiens, suggesting that this protein is widely distributed in eukaryotes. We describe here the crystal structures of the N-terminal single-stranded DNA (ssDNA)-binding domain of O. nova telomere end-binding protein alpha subunit both uncomplexed and complexed with single strand telomeric DNA. These structures show how the N-terminal domain of alpha alone, in the absence of the beta subunit and without alpha dimerization, can bind single-stranded telomeric DNA in a sequence-specific and 3'-end-specific manner. Furthermore, comparison of the uncomplexed and complexed forms of this protein shows that the ssDNA-binding site is largely pre-organized in the absence of ssDNA with modest, but interesting, rearrangements of amino acid side-chains that compose the ssDNA-binding site. The structures described here extend our understanding of structures of O. nova telomeric complexes by adding uncomplexed and complexed forms of monomeric alpha to previously described structures for (alpha 56/ssDNA)(2) dimer and alpha 56/beta 28/ssDNA ternary complexes. We believe that each of these four structures represent intermediates in an ordered assembly/disassembly pathway for O. nova telomeric complexes.
==About this Structure==
==About this Structure==
-
1K8G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sterkiella_nova Sterkiella nova] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K8G OCA].
+
1K8G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sterkiella_nova Sterkiella nova] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8G OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Sterkiella nova]]
[[Category: Sterkiella nova]]
[[Category: Classen, S.]]
[[Category: Classen, S.]]
-
[[Category: Ruggles, J.A.]]
+
[[Category: Ruggles, J A.]]
-
[[Category: Schultz, S.C.]]
+
[[Category: Schultz, S C.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: 3'-dna end binding protein]]
[[Category: 3'-dna end binding protein]]
Line 26: Line 26:
[[Category: telomeres]]
[[Category: telomeres]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:57:07 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:18 2008''

Revision as of 11:31, 21 February 2008


1k8g, resolution 2.6Å

Drag the structure with the mouse to rotate

Crystal Structure of the N-terminal domain of Oxytricha nova telomere end binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA

Overview

Oxytricha nova telomere end-binding protein specifically recognizes and caps single strand (T(4)G(4))(n) telomeric DNA at the very 3'-ends of O. nova macronuclear chromosomes. Proteins homologous to the N-terminal domain of OnTEBP alpha subunit have now been identified in Oxytricha trifallax, Stylonychia mytilis, Euplotes crassus, Schizosaccharomyces pombe, and Homo sapiens, suggesting that this protein is widely distributed in eukaryotes. We describe here the crystal structures of the N-terminal single-stranded DNA (ssDNA)-binding domain of O. nova telomere end-binding protein alpha subunit both uncomplexed and complexed with single strand telomeric DNA. These structures show how the N-terminal domain of alpha alone, in the absence of the beta subunit and without alpha dimerization, can bind single-stranded telomeric DNA in a sequence-specific and 3'-end-specific manner. Furthermore, comparison of the uncomplexed and complexed forms of this protein shows that the ssDNA-binding site is largely pre-organized in the absence of ssDNA with modest, but interesting, rearrangements of amino acid side-chains that compose the ssDNA-binding site. The structures described here extend our understanding of structures of O. nova telomeric complexes by adding uncomplexed and complexed forms of monomeric alpha to previously described structures for (alpha 56/ssDNA)(2) dimer and alpha 56/beta 28/ssDNA ternary complexes. We believe that each of these four structures represent intermediates in an ordered assembly/disassembly pathway for O. nova telomeric complexes.

About this Structure

1K8G is a Single protein structure of sequence from Sterkiella nova with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA., Classen S, Ruggles JA, Schultz SC, J Mol Biol. 2001 Dec 14;314(5):1113-25. PMID:11743727

Page seeded by OCA on Thu Feb 21 13:31:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools