3hl8 | pdb_00003hl8

Crystal structure of exonuclease I in complex with inhibitor BCBP

spinqualitylabelsall models 3hl8, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hl8 is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BBP, DMS, EDO, MG Related: 3c95, 3c94, 3hp9 Gene: b2011, cpeA, JW1993, sbcB, xonA (ECOLI) Activity: Exodeoxyribonuclease I, with EC number 3.1.11.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EX1_ECOLI] Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease AP lyase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacterial single-stranded DNA-binding proteins (SSBs) help to recruit a diverse array of genome maintenance enzymes to their sites of action through direct protein interactions. For all cases examined to date, these interactions are mediated by the evolutionarily conserved C terminus of SSB (SSB-Ct). The essential nature of SSB protein interactions makes inhibitors that block SSB complex formation valuable biochemical tools and attractive potential antibacterial agents. Here, we identify four small molecules that disrupt complexes formed between Escherichia coli SSB and Exonuclease I (ExoI), a well-studied SSB-interacting enzyme. Each compound disrupts ExoI/SSB-Ct peptide complexes and abrogates SSB stimulation of ExoI nuclease activity. Structural and biochemical studies support a model for three of the compounds in which they compete with SSB for binding to ExoI. The fourth appears to rely on an allosteric mechanism to disrupt ExoI/SSB complexes. Subsets of the inhibitors block SSB-Ct complex formation with two other SSB-interaction partners as well, which highlights their utility as reagents for investigating the roles of SSB/protein interactions in diverse DNA replication, recombination, and repair reactions. Small-molecule tools for dissecting the roles of SSB/protein interactions in genome maintenance.,Lu D, Bernstein DA, Satyshur KA, Keck JL Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):633-8. Epub 2009 Dec 16. PMID:20018747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exonuclease 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA