1f2t: Difference between revisions

Revision as of 02:27, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f2t.png

Template:STRUCTURE 1f2t

CRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASECRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASE

Template:ABSTRACT PUBMED 10892749

About this StructureAbout this Structure

1F2T is a Protein complex structure of sequences from Pyrococcus furiosus. 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 Tue Jul 1 02:27:30 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASE'''
+===CRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASE===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10892749}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10892749 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10892749}}
 ==About this Structure==
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 [[Category: Abc atpase]]
 [[Category: Dna double-strand break repair]]
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