1F05

CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE

Summary for 1F05

• Entry DOI: 10.2210/pdb1f05/pdb
• Related: 1ONR 1UCW
• Descriptor: TRANSALDOLASE (2 entities in total)
• Functional Keywords: alpha-beta barrel, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P37837
• Total number of polymer chains: 2
• Total formula weight: 75182.21

Authors

Schneider, G.,Thorell, S. (deposition date: 2000-05-14, release date: 2000-07-13, Last modification date: 2023-08-09)

Primary citation

Thorell, S.,Gergely Jr., P.,Banki, K.,Perl, A.,Schneider, G.
The three-dimensional structure of human transaldolase.
FEBS Lett., 475:205-208, 2000

PubMed Abstract: The crystal structure of human transaldolase has been determined to 2.45 A resolution. The enzyme folds into an alpha/beta barrel structure and is thus similar in structure to other class I aldolases. Structure-based sequence alignment of available sequences of the transaldolase subfamily reveals that eight active site residues are invariant in the whole subfamily. Other invariant residues are mainly involved in the formation of the hydrophobic core of the enzyme. Noteworthy is a hydrophobic cluster consisting of five invariant residues. Human transaldolase has been implicated as an autoantigen in multiple sclerosis and four immunodominant peptide segments are located at the surface of the enzyme, accessible to autoantibodies.

PubMed: 10869557
DOI: 10.1016/S0014-5793(00)01658-6

Experimental method

X-RAY DIFFRACTION (2.45 Å)