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The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.

Abstract：

:The crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The crystallographic asymmetric unit contains two monomers related by approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is built up by crystallographic symmetry. The tetramer is almost planar with no contacts between the subunits related by the non-crystallographic dyad. The active sites are accessible from a wide water-filled channel in the center of the tetramer. The dihydrodipicolinate synthase monomer is composed of two domains. Each polypeptide chain is folded into an 8-fold alpha/beta barrel and a C-terminal alpha-helical domain comprising residues 224 to 292. The fold is similar to that of N-acetylneuraminate lyase. The active site lysine 161 is located in the alpha/beta barrel and has access via two entrances from the C-terminal side of the barrel.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Mirwaldt C,Korndörfer I,Huber R

doi

10.1006/jmbi.1994.0078

subject

Has Abstract

pub_date

1995-02-10 00:00:00

pages

227-39

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(84)70078-7

journal_volume

246

pub_type

杂志文章

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