2FK5

Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8

Summary for 2FK5

• Entry DOI: 10.2210/pdb2fk5/pdb
• Related: 2FLF
• Descriptor: fuculose-1-phosphate aldolase, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: class ii aldolase, metal binding, fuculose phosphate, riken structural genomics/proteomics initiative, rsgi, nppsfa, national project on protein structural and functional analyses, lyase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 43575.51

Authors

Jeyakanthan, J.,Shiro, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-01-04, release date: 2007-01-04, Last modification date: 2023-10-25)

Primary citation

Jeyakanthan, J.,Taka, J.,Kikuchi, A.,Kuroishi, C.,Yutani, K.,Shiro, Y.
Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8
Acta Crystallogr.,Sect.F, 61:1075-1077, 2005

PubMed 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.

PubMed: 16511238
DOI: 10.1107/S1744309105036766

Experimental method

X-RAY DIFFRACTION (1.9 Å)