CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS

Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.

Changes in the Catalytic Properties of P-Hydroxybenzoate Hydroxylase Caused by the Mutation Asn300Asp

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENFVGLPYEEIE

ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON DSSP OUTPUT
(KABSCH AND SANDER, 1983).

THE HYDROGEN BOND DISTANCE CUTOFF USED FOR THE TURNS IS
3.5 ANGSTROMS. THE CA(X) TO CA(X+4) DISTANCE IS LESS THAN
6.0 ANGSTROMS. THE ANGLES ARE FROM ROBSON AND GARNIER
(1986) 'INTRODUCTION TO PROTEINS AND PROTEIN ENGINEERING',
ELSEVIER, AMSTERDAM.
TYPE PHI2 PSI2 PHI3 PSI3
I -75(+-65) -30(+-40) -90(+-40) -15 TO 40
II -60(+-40) 120(+-40) 90(+-40) 0(+-40)
III -75(+-65) -30(+-40) -60(+-40) -15 TO -70
I(PRIME) 75(+-65) 30(+-40) 90(+-40) -40 TO 15
II(PRIME) 60(+-40) -120(+-40) -90(+-40) 0(+-40)
III(PRIME) 75(+-65) 30(+-40) 60(+-40) 15 TO 70

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE