1f2u: Difference between revisions

Revision as of 13:34, 21 February 2008

CRYSTAL STRUCTURE OF RAD50 ABC-ATPASE

OverviewOverview

To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd displays ATPase activity plus ATP-controlled dimerization and DNA binding activities. Rad50cd crystal structures identify probable protein and DNA interfaces and reveal an ABC-ATPase fold, linking Rad50 molecular mechanisms to ABC transporters, including P glycoprotein and cystic fibrosis transmembrane conductance regulator. Binding of ATP gamma-phosphates to conserved signature motifs in two opposing Rad50cd molecules promotes dimerization that likely couples ATP hydrolysis to dimer dissociation and DNA release. These results, validated by mutations, suggest unified molecular mechanisms for ATP-driven cooperativity and allosteric control of ABC-ATPases in DSBR, membrane transport, and chromosome condensation by SMC proteins.

About this StructureAbout this Structure

1F2U is a Protein complex structure of sequences from Pyrococcus furiosus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily., Hopfner KP, Karcher A, Shin DS, Craig L, Arthur LM, Carney JP, Tainer JA, Cell. 2000 Jun 23;101(7):789-800. PMID:10892749

Page seeded by OCA on Thu Feb 21 12:34:10 2008

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OCA

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-[[Image:1f2u.jpg|left|200px]]<br /><applet load="1f2u" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f2u.jpg|left|200px]]<br /><applet load="1f2u" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f2u, resolution 1.6&Aring;" />
 '''CRYSTAL STRUCTURE OF RAD50 ABC-ATPASE'''<br />
 ==Overview==
-To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we biochemically and structurally characterized ATP-bound and ATP-free, Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd, displays ATPase activity plus ATP-controlled dimerization and DNA binding, activities. Rad50cd crystal structures identify probable protein and DNA, interfaces and reveal an ABC-ATPase fold, linking Rad50 molecular, mechanisms to ABC transporters, including P glycoprotein and cystic, fibrosis transmembrane conductance regulator. Binding of ATP, gamma-phosphates to conserved signature motifs in two opposing Rad50cd, molecules promotes dimerization that likely couples ATP hydrolysis to, dimer dissociation and DNA release. These results, validated by mutations, suggest unified molecular mechanisms for ATP-driven cooperativity and, allosteric control of ABC-ATPases in DSBR, membrane transport, and, chromosome condensation by SMC proteins.
+To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd displays ATPase activity plus ATP-controlled dimerization and DNA binding activities. Rad50cd crystal structures identify probable protein and DNA interfaces and reveal an ABC-ATPase fold, linking Rad50 molecular mechanisms to ABC transporters, including P glycoprotein and cystic fibrosis transmembrane conductance regulator. Binding of ATP gamma-phosphates to conserved signature motifs in two opposing Rad50cd molecules promotes dimerization that likely couples ATP hydrolysis to dimer dissociation and DNA release. These results, validated by mutations, suggest unified molecular mechanisms for ATP-driven cooperativity and allosteric control of ABC-ATPases in DSBR, membrane transport, and chromosome condensation by SMC proteins.
 ==About this Structure==
-F2U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F2U OCA].
+F2U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2U OCA].
 ==Reference==
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 [[Category: Pyrococcus furiosus]]
 [[Category: Craig, L.]]
-[[Category: Hopfner, K.P.]]
+[[Category: Hopfner, K P.]]
 [[Category: Karcher, A.]]
-[[Category: Shin, D.S.]]
+[[Category: Shin, D S.]]
 [[Category: ATP]]
 [[Category: MG]]
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 [[Category: dna double-strand break repair]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:33:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:10 2008''