1ph2: Difference between revisions

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[[Image:1ph2.gif|left|200px]]<br /><applet load="1ph2" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ph2.gif|left|200px]]
caption="1ph2, resolution 3.10&Aring;" />
 
'''CRYSTAL STRUCTURE OF THE OXYTRICHA NOVA TELOMERE END-BINDING PROTEIN COMPLEXED WITH NONCOGNATE SSDNA GGGGTTTTG'''<br />
{{Structure
|PDB= 1ph2 |SIZE=350|CAPTION= <scene name='initialview01'>1ph2</scene>, resolution 3.10&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
|ACTIVITY=
|GENE= MAC-56A AND MAC-56K AND MAC-56S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=200597 Sterkiella nova]), MAC-41A AND MAC-41S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=200597 Sterkiella nova])
}}
 
'''CRYSTAL STRUCTURE OF THE OXYTRICHA NOVA TELOMERE END-BINDING PROTEIN COMPLEXED WITH NONCOGNATE SSDNA GGGGTTTTG'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1PH2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sterkiella_nova Sterkiella nova] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PH2 OCA].  
1PH2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sterkiella_nova Sterkiella nova]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PH2 OCA].  


==Reference==
==Reference==
Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes., Theobald DL, Schultz SC, EMBO J. 2003 Aug 15;22(16):4314-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12912928 12912928]
Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes., Theobald DL, Schultz SC, EMBO J. 2003 Aug 15;22(16):4314-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12912928 12912928]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sterkiella nova]]
[[Category: Sterkiella nova]]
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[[Category: ob fold]]
[[Category: ob fold]]
[[Category: oligonucleotide and oligosaccharide binding fold]]
[[Category: oligonucleotide and oligosaccharide binding fold]]
[[Category: protein dna interactions]]
[[Category: protein dna interaction]]
[[Category: protein/dna]]
[[Category: protein/dna]]
[[Category: sequence specificity]]
[[Category: sequence specificity]]
[[Category: single strand dna binding protein]]
[[Category: single strand dna binding protein]]
[[Category: telomeres]]
[[Category: telomere]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:24:13 2008''

Revision as of 14:24, 20 March 2008

File:1ph2.gif


PDB ID 1ph2

Drag the structure with the mouse to rotate
, resolution 3.10Å
Ligands: and
Gene: MAC-56A AND MAC-56K AND MAC-56S (Sterkiella nova), MAC-41A AND MAC-41S (Sterkiella nova)
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE OXYTRICHA NOVA TELOMERE END-BINDING PROTEIN COMPLEXED WITH NONCOGNATE SSDNA GGGGTTTTG


OverviewOverview

Sequence-specific protein recognition of single-stranded nucleic acids is critical for many fundamental cellular processes, such as DNA replication, DNA repair, transcription, translation, recombination, apoptosis and telomere maintenance. To explore the mechanisms of sequence-specific ssDNA recognition, we determined the crystal structures of 10 different non-cognate ssDNAs complexed with the Oxytricha nova telomere end-binding protein (OnTEBP) and evaluated their corresponding binding affinities (PDB ID codes 1PH1-1PH9 and 1PHJ). The thermodynamic and structural effects of these sequence perturbations could not have been predicted based solely upon the cognate structure. OnTEBP accommodates non-cognate nucleotides by both subtle adjustments and surprisingly large structural rearrangements in the ssDNA. In two complexes containing ssDNA intermediates that occur during telomere extension by telomerase, entire nucleotides are expelled from the complex. Concurrently, the sequence register of the ssDNA shifts to re-establish a more cognate-like pattern. This phenomenon, termed nucleotide shuffling, may be of general importance in protein recognition of single-stranded nucleic acids. This set of structural and thermodynamic data highlights a fundamental difference between protein recognition of ssDNA versus dsDNA.

About this StructureAbout this Structure

1PH2 is a Protein complex structure of sequences from Sterkiella nova. Full crystallographic information is available from OCA.

ReferenceReference

Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes., Theobald DL, Schultz SC, EMBO J. 2003 Aug 15;22(16):4314-24. PMID:12912928

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