The crystal structure of the adenylation enzyme VinN reveals a unique beta-amino acid recognition mechanism

Numerical link type Si(111) double crystal monochromator

MNHKVHHHHHHIEGRHMYSPDRRAALNSVANMVSDNADKDLRYGGLVHDLLADSGKATPNSDAMEDAFGTWTYQELLNHS
QAFSAWLDGKGVARGERIVVQLPNIRQTVAVFYGACRRGVVFVPLNPGMKPFHLRSVIADADPRLVIAEDETAADRLRDV
TDLPVYSIDSLWADVERLRDAGAGAEAVEVSPEDLAVLIYTSGSTAAPKAVACPHQQIVFAASSINAVLGYHAEDIVFCR
MSVSWDFGLYKVLISTLTGAKLVLAGGEPDIALVKSLRESGATMMPIVPSLASMLTTLIRRDPEGAPTLRMFTNSAAALP
QVTIDALRSAFPGAQVVRMYGQTECKRISIMPPHLEHERPDSVGLPLPGTTIEILDEDGTLLPPGEPGEITVTGPHVMAG
YWRAPEITARAYRRDETTGAMRLHTGDYGHLDEDGFLYFGGR

0.1M Tris-HCl, 0.2M sodium acetate, 30% polyethylene glycol 4000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 278K

U VALUES: WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Five-layered alpha-beta-alpha-beta-alpha sandwich fold, Ligase, ATP binding

MEDAFGTWTYQELLNHSQAFSAWLDGKGVARGERIVVQLPNIRQTVAVFYGACRRGVVFVPLNPGMKPFHLRSVIADADP
RLVIAEDETAADRLRDVTDLPVYSIDSLWADVERLRDAGAGAEAVEVSPEDLAVLIYTSGSTAAPKAVACPHQQIVFAAS
SINAVLGYHAEDIVFCRMSVSWDFGLYKVLISTLTGAKLVLAGGEPDIALVKSLRESGATMMPIVPSLASMLTTLIRRDP
EGAPTLRMFTNSAAALPQVTIDALRSAFPGAQVVRMYGQTECKRISIMPPHLEHERPDSVGLPLPGTTIEILDEDGTLLP
PGEPGEITVTGPHVMAGYWRAPEITARAYRRDETTGAMRLHTGDYGHLDEDGFLYFGGR