1svm

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[[Image:1svm.gif|left|200px]]
[[Image:1svm.gif|left|200px]]
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{{Structure
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|PDB= 1svm |SIZE=350|CAPTION= <scene name='initialview01'>1svm</scene>, resolution 1.94&Aring;
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The line below this paragraph, containing "STRUCTURE_1svm", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1svm| PDB=1svm | SCENE= }}
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|RELATEDENTRY=[[1svl|1SVL]], [[1svo|1SVO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svm OCA], [http://www.ebi.ac.uk/pdbsum/1svm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svm RCSB]</span>
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'''Co-crystal structure of SV40 large T antigen helicase domain and ATP'''
'''Co-crystal structure of SV40 large T antigen helicase domain and ATP'''
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[[Category: Gai, D.]]
[[Category: Gai, D.]]
[[Category: Zhao, R.]]
[[Category: Zhao, R.]]
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[[Category: aaa+ fold]]
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[[Category: Aaa+ fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:32 2008''
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Revision as of 06:11, 3 May 2008

Image:1svm.gif


PDB ID 1svm

Drag the structure with the mouse to rotate
1svm, resolution 1.94Å ()
Ligands: , ,
Related: 1svl, 1svo
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Co-crystal structure of SV40 large T antigen helicase domain and ATP


Overview

The large tumor antigen (LTag) of simian virus 40, an AAA(+) protein, is a hexameric helicase essential for viral DNA replication in eukaryotic cells. LTag functions as an efficient molecular machine powered by ATP binding and hydrolysis for origin DNA melting and replication fork unwinding. To understand how ATP binding and hydrolysis are coupled to conformational changes, we have determined high-resolution structures ( approximately 1.9 A) of LTag hexamers in distinct nucleotide binding states. The structural differences of LTag in various nucleotide states detail the molecular mechanisms of conformational changes triggered by ATP binding/hydrolysis and reveal a potential mechanism of concerted nucleotide binding and hydrolysis. During these conformational changes, the angles and orientations between domains of a monomer alter, creating an "iris"-like motion in the hexamer. Additionally, six unique beta hairpins on the channel surface move longitudinally along the central channel, possibly serving as a motor for pulling DNA into the LTag double hexamer for unwinding.

About this Structure

1SVM is a Single protein structure of sequence from Simian virus 40. The following page contains interesting information on the relation of 1SVM with [AAA+ Proteases]. Full crystallographic information is available from OCA.

Reference

Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen., Gai D, Zhao R, Li D, Finkielstein CV, Chen XS, Cell. 2004 Oct 1;119(1):47-60. PMID:15454080 Page seeded by OCA on Sat May 3 09:11:18 2008

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