STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3,4-DIHYDROXYBENZOATE

Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding.

Structures of Competitive Inhibitor Complexes of Protocatechuate 3,4-Dioxygenase: Multiple Exogenous Ligand Binding Orientations within the Active Site

Structure of Protocatechuate 3,4-Dioxygenase from Pseudomonas Aeruginosa at 2.15 A Resolution

Structure and Assembly of Protocatechuate 3,4-Dioxygenase

PREVIOUSLY CLASSIFIED AS PSEUDOMONAS AERUGINOSA

THE ENTRY COORDINATES
ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.

TWO SUBSTRATE MOLECULES BIND TO EACH PROTOMER; ONE IN THE ACTIVE SITE (RESIDUE 550) AND ONE NEAR THE LOCAL THREE-FOLD SYMMETRY AXIS (RESIDUE 551).

THE NONSTANDARD UNIT CELL I 2 WAS CHOSEN OVER THE
EQUIVALENT C 2 CELL BECAUSE OF THE CONVENIENCE OF HAVING A
BETA ANGLE NEAR 90 DEGREES AND TO MAINTAIN CONSISTENCY WITH
THE INITIAL CRYSTALLIZATION REPORT. TO CONVERT FROM
FRACTIONAL I 2 TO FRACTIONAL C 2, USE THE FOLLOWING
TRANSFORMATION:

[ 1.0 ][ 0.0 ][ 0.0 ] (XFRAC_I2) (XFRAC_C2)
[ 0.0 ][ 1.0 ][ 0.0 ] X (YFRAC_I2) = (YFRAC_C2)
[ -1.0 ][ 0.0 ][ 1.0 ] (ZFRAC_I2) (ZFRAC_C2)

THE ORTHOGONAL COORDINATE SYSTEM CHOSEN FOR THIS ENTRY
IS THAT DEFINED BY THE LOCAL SYMMETRY OF THE COMPLEX (23).

PROTOCATECHUATE 3,4-DIOXYGENASE, BETA-MERCAPTOETHANOL, 3,4-DIHYDROXYBENZOIC ACID

THE ACTIVE FORM OF THE ENZYME IS THE WHOLE UNIT CELL
CONTENT. IT CONSISTS OF 12 PROTOMERS. EACH PROTOMER IS
MADE OF TWO POLYPEPTIDE CHAINS AND ONE FE(III). THE
ASYMMETRIC UNIT CONSISTS OF 6 PROTOMERS. THEY ARE: CHAINS
(A, M), CHAINS (B, N), CHAINS (C, O), CHAINS (D, P), CHAINS
(E, Q), CHAINS (F, R). EACH PROTOMER CONTAINS AN ACTIVE
SITE WITH FE(III) AS THE CENTER AND A VESTIGIAL SITE. THE
ACTIVE SITES ARE NAMED: ACA, ACB, ACC, ACD, ACE, ACF. THE
VESTIGIAL SITES ARE NAMED VEA, VEB, VEC, VED, VEE AND VEF.
THE CHAIN IDENTIFIERS HAVE BEEN ASSIGNED AS FOLLOWS:

ALPHA BETA WATERS
A M G
B N H
C O I
D P J
E Q K
F R L

DIOXYGENASE, IRON, NONHEME, METALLOPROTEIN, OXIDOREDUCTASE, SUBSTRATE COMPLEX
SITE "ACA" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M.
SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N.
SITE "ACC" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O.
SITE "ACD" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P.
SITE "ACE" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q.
SITE "ACF" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R.
SITE "VEA" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M.
SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N.
SITE "VEC" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O.
SITE "VED" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P.
SITE "VEE" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q.
SITE "VEF" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R.
SECONDARY THREE-FOLD SITE BETWEEN M, N, O CHAINS.
SECONDARY THREE-FOLD SITE BETWEEN P, Q, R CHAINS.