1. Learning Our ABCs: Rad50 Directs MRN Repair Functions via Adenylate Kinase Activity from the Conserved ATP Binding Cassette 
R. Scott Williams, John A. Tainer 
Molecular Cell 
Volume 25, Issue 6, Pages (March 2007)
DOI: /j.molcel
Copyright © 2007 Elsevier Inc. Terms and Conditions

2. Figure 1
Structural and Catalytic Features of ATP Binding Cassette Proteins
(A) X-ray crystal structures AMP-PNP (a nonhydrolysable ATP analog) complexes of Pyrococcus furiosus Rad50 ABC ATPase (RCSB code 1F2U) and the murine CFTR ABC ATPase nucleotide binding domain 1 (NBD1) (RCSB code 1Q3H). Conserved Walker A, Walker B, ABC signature motif, D loops, and Q loops are highlighted.
(B) ATP-dependant reactions catalyzed by the Rad50 ABC ATPase/adenylate kinase domains. Ap5A, which covalently links the ATP (red) and AMP (blue) AK substrate nucleotides through an additional phosphate group, is a specific inhibitor of the reversible adenylate kinase reaction.
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2007 Elsevier Inc. Terms and Conditions