1svm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1svm |SIZE=350|CAPTION= <scene name='initialview01'>1svm</scene>, resolution 1.94Å | |PDB= 1svm |SIZE=350|CAPTION= <scene name='initialview01'>1svm</scene>, resolution 1.94Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1svl|1SVL]], [[1svo|1SVO]] | |||
|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> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Gai, D.]] | [[Category: Gai, D.]] | ||
[[Category: Zhao, R.]] | [[Category: Zhao, R.]] | ||
[[Category: aaa+ fold]] | [[Category: aaa+ fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:32 2008'' | ||
Revision as of 23:47, 30 March 2008
| |||||||
| , resolution 1.94Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1SVL, 1SVO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Co-crystal structure of SV40 large T antigen helicase domain and ATP
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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 Sun Mar 30 23:47:32 2008