Engineering the enolase active site pocket: Crystal structure of the S39N D321R mutant of yeast enolase 1

Engineering the Enolase Magnesium II Binding Site -Implications for its Evolution.

2-PHOSPHOGLYCERATE DEHYDRATASE, 1,2-PHOSPHO-D-GLYCERATE HYDRO-LYASE 1

AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGANTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKAN
IDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHA
GGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGK
IKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVAD
RLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKLLHHHHHH

20% PEG 8000, 0.2M SODIUM ACETATE, 0.1M SODIUM CACODYLATE PH 6.5

ENGINEERING THE ENOLASE ACTIVE SITE POCKET: CRYSTAL STRUCTURE OF THE S39N D321A MUTANT OF YEAST ENOLASE 1

REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASECATALYSIS IN ENOLASE

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) COMPLEXED WITH PHOSPHONOACETOHYDROXAMATE AND MANGANESE

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) (APO FORM)

MG-PHOSPHONOACETOHYDROXAMATE COMPLEX OF S39A YEAST ENOLASE 1

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) (APO)

ENGINEERING THE ENOLASE ACTIVE SITE POCKET: CRYSTAL STRUCTURE OF THE S39N Q167K D321R MUTANT OF YEAST ENOLASE 1

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) (HOLO)

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) COMPLEX WITH 2-PHOSPHO-D-GLYCERIC ACID AND CALCIUM

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) COMPLEX WITH ORTHOPHOSPHATE, FLUORIDE AND MAGNESIUM

ASYMMETRIC YEAST ENOLASE DIMER COMPLEXED WITH RESOLVED 2'-PHOSPHOGLYCERATE AND PHOSPHOENOLPYRUVATE

ENGINEERING THE ENOLASE ACTIVE SITE POCKET: CRYSTAL STRUCTURE OF THE D321A MUTANT OF YEAST ENOLASE 1

ENGINEERING THE ENOLASE ACTIVE SITE POCKET: CRYSTAL STRUCTURE OF THE S39A D321A MUTANT OF YEAST ENOLASE 1

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) COMPLEX WITH PHOSPHOGLYCOLIC ACID AND ZINC

YEAST ENOLASE COMPLEXED WITH AN EQUILIBRIUM MIXTURE OF 2'-PHOSPHOGLYCEATE AND PHOSPHOENOLPYRUVATE

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) COMPLEX WITH 2-PHOSPHO-D-GLYCERIC ACID AND MAGNESIUM

ENOLASE (2-PHOSPHO-D-GLYCERATE HYDROLASE) COMPLEXED WITH MG 2+

CRYSTAL STRUCTURE ANALYSIS OF ENOLASE MG SUBUNIT COMPLEX AT PH 8.0

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

ENGINEERED RESIDUE IN CHAIN A, SER 40 TO ASN ENGINEERED RESIDUE IN CHAIN A, ASP 322 TO ARG ENGINEERED RESIDUE IN CHAIN B, SER 40 TO ASN ENGINEERED RESIDUE IN CHAIN B, ASP 322 TO ARG

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

LYASE, TIM-BARREL, GLYCOLYSIS, GLUCONEOGENESIS, METAL BINDING, ENOLASE SUPERFAMILY