Crystal structure of mutant R322A of beta-alanine synthase from Saccharomyces kluyveri

N-CARBAMYL-BETA-ALANINE; BETA-UREIDOPROPIONATE

Crystal Structures of Yeast -Alanine Synthase Complexes Reveal the Mode of Substrate Binding and Large Scale Domain Closure Movements.

Yeast Beta-Alanine Synthase Shares a Structural Scaffold and Origin with Dizinc-Dependent Exopeptidases

Crystallization and Preliminary X-Ray Analysis of Beta-Alanine Synthase from the Yeast Saccharomyces Kluyveri

SKDVSSTITTVSASPDGTLNLPAAAPLSIASGRLNQTILETGSQFGGVARWGQESHEFGMRRLAGTALDGAMRDWFTNEC
ESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEG
ARFARSCTGSSVWSHDLSLEEAYGLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEIDAHFELHIEQGPILEDENKAIG
IVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDF
AHPSDDVLATMLKEAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIWSGAGHDSCQ
TAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAIINYDNYRVIRGHQFPGDDDDKHHHHHHHHSGD

TRISODIUM CITRATE PH 6.0, DIOXANE,ACETONE, DTT, NA-HEPES PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K

CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROMSACCHAROMYCES KLUYVERI

CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROMSACCHAROMYCES KLUYVEI (SELENOMETHIONINE SUBSTITUTEDPROTEIN)

CRYSTAL STRUCTURE OF MUTANT E159A OF BETA- ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI

CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE PRODUCT BETA-ALANINE

CRYSTAL STRUCTURE OF MUTANT E159A OF BETA- ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH ITS SUBSTRATE N-CARBAMYL- BETA-ALANINE

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

ENGINEERED RESIDUE IN CHAIN A, ARG 322 TO ALA ENGINEERED RESIDUE IN CHAIN B, ARG 322 TO ALA ENGINEERED RESIDUE IN CHAIN C, ARG 322 TO ALA ENGINEERED RESIDUE IN CHAIN D, ARG 322 TO ALA
1,4-DITHIOTHREITOL (DTT): C 503 IS CONNECTED BY A DISULFIDE BRIDGE TO CYS 168 IN CHAIN C
THE N-TERMINAL METHIONINE IS ABSENT, MOST LIKELY DUE TO POSTTRANSLATIONAL MODIFICATION, THE LAST 20 AMINO ACIDS CORRESPOND TO THE C-TERMINAL HIS-TAG, R322 OF THE DEPOSITED SEQUENCE IS REPLACED BY ALANINE IN THIS MUTANT

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

HYDROLASE, DI-ZINC CENTER, AMIDOHYDROLASE, ALPHA AND BETA PROTEIN