CATALYTIC METAL ION BINDING IN ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MN2+-PHOSPHONOACETOHYDROXAMATE COMPLEX AT 2.4 ANGSTROMS RESOLUTION

Catalytic metal ion binding in enolase: the crystal structure of an enolase-Mn2+-phosphonoacetohydroxamate complex at 2.4-A resolution.

Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-Mg2+-F--PI Complex at 2.6-Angstroms Resolution

Mechanism of Enolase: The Crystal Structure of Enolase-Mg2+-Phosphoglycerate(Slash) Phosphoenolpyruvate Complex at 2.2-Angstroms Resolution

Inhibition of Enolase: The Crystal Structures of Enolase-Ca2+-Phosphoglycerate and Enolase-Zn2+-Phosphoglycolate Complexes at 2.2-Angstroms Resolution

Refined Structure of Yeast Apo-Enolase at 2.25 Angstroms Resolution

Crystal Structure of Holoenzyme Refined at 1.9 Angstroms Resolution: Trigonal-Bipyramidal Geometry of the Cation Binding Site

The Structure of Yeast Enolase at 2.25-Angstroms Resolution. An 8-Fold Beta+Alpha-Barrel with a Novel Beta Beta Alpha Alpha (Beta Alpha)6 Topology

Crystal Structure of Enolase Indicates that Enolase and Pyruvate Kinase Evolved from a Common Ancestor

Crystallization and Preliminary Crystallographic Data for a Tetragonal Form of Yeast Enolase

AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKAN
IDVSDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHA
GGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGK
VKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVAD
DLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL

SHEET
THE SHEET PRESENTED AS *BAR* ON SHEET RECORDS BELOW IS
ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS
REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND
LAST STRANDS ARE IDENTICAL. THERE IS A SMALL STRAND BONDED
TO THE END OF STRAND 1 OF THE BARREL. THIS SMALL STRAND
AND STRAND 1 ARE PRESENTED AS SHEET *S1*.

SEQUENCE ADVISORY NOTICE:
DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.

SWISS-PROT ENTRY NAME: ENO1_YEAST

SWISS-PROT RESIDUE PDB SEQRES
NAME NUMBER NAME CHAIN SEQ/INSERT CODE
LYS 84 SER 84

AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKAN
IDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHA
GGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGK
VKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVAD
DLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL

ACTIVE SITE RESIDUES THAT ARE PROBABLY INVOLVED IN SUBSTRATE BINDING AND CATALYSIS