Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl] adenosine

5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl] adenosine

Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.

Side-scattering cuberoot I-beam bent single crystal; asymetric cut 12.2 degs

GHMKKQLIEFVRWSPERAQHYRNKGYWIDQPLTRILTVGVQSHPHSLAIICGERQLSYIELDRLSTNLATRLAEKGLGKG
DTALVQLPNVAEFYIVFFALLKAGVVVLNALYSHRQYELNAFIKQIQPKLLIGSRQHEVFSNNQFIDSLHDVNLSPEIIL
MLNHQATDFGLLDWIETPAETFVDFSSTPADEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICGLNSNTRLLCALP
APHNFMLSSPGALGVLHAGGCVVMAPNPEPLNCFSIIQRHQVNMASLVPSAVIMWLEKAAQYKDQIQSLKLLQVGGASFP
ESLARQVPEVLNCKLQQVFGMAEGLVNYTRLDDSDEQIFTTQGRPISSDDEIKIVDEQYREVPEGEIGMLATRGPYTFCG
YYQSPEHNSQVFDEDNYYYSGDLVQRTPDGNLRVVGRIKDQINRGGEKIASEEIEKLILLHPEVMHAALVAIVDEQFGEK
SCAFIVSRNPELKAVVLRRHLMELGIAQYKLPDQIKLIESLPLTAVGKVDKKQLRSILNTSTTS

5-15% PEG 8000, 5% MPD, 250-600 mM CaCl2, 50 mM BTP, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 287K

THIS ENTRY USES A UNIPROT REFERENCE THAT IS FOR A DIFFERENT STRAIN OF A. BAUMANNI. THESE CHANGES ARE STRAIN RELATED DIFFERENCES AS FOUND IN GENBANK ENTRY ZP_04661818.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Ligase, Adenylation of 2, 3-dihydroxybenzoate and transfer to pantetheine cofactor of BasF, Non-Ribosomal Peptide Synthetase (NRPS)

MKKQLIEFVRWSPERAQHYRNKGYWIDQPLTRILTVGVQSHPHSPAIICGERQLSYIELDRLSTNLASRLAEKGLGKGDT
ALVQLPNVAEFYIVFFALLKAGVVVLNALYSHRQYELNAFIKQIQPKLLIGSRQHEVFSNNQFIDSLHEVNLSPEIILML
NHQATDFGLLDWIETPAETLVDFSSTPADEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICDLNSNTRLLCALPAP
HNFMLSSPGALGVLHAGGCVVMAPNPEPLNCFSIIQRHQVNMASLVPSAVIMWLEKAAQYKDQIQSLKLLQVGGASFPES
LARQVPEVINCKLQQVFGMAEGLVNYTRLDDSDEQIFTTQGRPISSDDEIKIVDEQYKEVPEGEIGMLATRGPYTFCGYY
QSPEHNSQVFDEDNYYYSGDLVQRTPDGNLRVVGRIKDQINRGGEKIASEEIEKLILLHPEVMHAALVAIVDEQFGEKSC
AFIVSRNPELKAVVLRRHLMELGIAQYKLPDQIKLIESLPLTAVGKVDKKQLRSILNTSTTS