PDBsum entry 2fk5

Lyase

PDB id: 2fk5

Contents

Protein chains

195 a.a. *

Ligands

SO4 ×2

Metals

_CL ×4

Waters ×335

* Residue conservation analysis

PDB id:

2fk5

Name:

Lyase

Title:

Crystal structure of l-fuculose-1-phosphate aldolase from thermus thermophilus hb8

Structure:

Fuculose-1-phosphate aldolase. Chain: a, b. Synonym: class ii aldolase protein. Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.190 R-free: 0.233

Authors:

J.Jeyakanthan,Y.Shiro,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

J.Jeyakanthan et al. (2005). Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8. Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 1075-1077. PubMed id: 16511238

Date:

04-Jan-06 Release date: 04-Jan-07

Protein chains

Q5SHB9  (Q5SHB9_THET8) -  Fuculose-1-phosphate aldolase from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 200 a.a.

Struc: 195 a.a.

Enzyme reactions

• Enzyme class: E.C.4.1.2.17 - L-fuculose-phosphate aldolase.
• Reaction: L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Acta Crystallogr Sect F Struct Biol Cryst Commun 61:1075-1077 (2005)

PubMed id: 16511238

Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8.

J.Jeyakanthan, J.Taka, A.Kikuchi, C.Kuroishi, K.Yutani, Y.Shiro.

ABSTRACT

Fuculose phosphate aldolase catalyzes the reversible cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. The protein from Thermus thermophilus HB8 is a biological tetramer with a subunit molecular weight of 21 591 Da. Purified FucA has been crystallized using sitting-drop vapour-diffusion and microbatch techniques at 293 K. The crystals belong to space group P4, with unit-cell parameters a = b = 100.94, c = 45.87 A. The presence of a dimer of the enzyme in the asymmetric unit was estimated to give a Matthews coefficient (VM) of 2.7 A3 Da(-1) and a solvent content of 54.2%(v/v). Three-wavelength diffraction MAD data were collected to 2.3 A from zinc-containing crystals. Native diffraction data to 1.9 A resolution have been collected using synchrotron radiation at SPring-8.