1TPF

COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS

Summary for 1TPF

• Entry DOI: 10.2210/pdb1tpf/pdb
• Descriptor: TRIOSEPHOSPHATE ISOMERASE, DIMETHYL SULFOXIDE (3 entities in total)
• Functional Keywords: isomerase(intramolecular oxidoreductase)
• Biological source: Trypanosoma brucei brucei
• Total number of polymer chains: 2
• Total formula weight: 54044.20

Authors

Radha Kishan, K.V.,Zeelen, J.Ph.,Wierenga, R.K. (deposition date: 1994-02-28, release date: 1994-05-31, Last modification date: 2024-02-14)

Primary citation

Kishan, K.V.,Zeelen, J.P.,Noble, M.E.,Borchert, T.V.,Wierenga, R.K.
Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Protein Sci., 3:779-787, 1994

PubMed Abstract: Triosephosphate isomerase (TIM) is a dimeric enzyme consisting of 2 identical subunits. Trypanosomal TIM can be crystallized in 4 different spacegroups: P2(1)2(1)2(1), C2(big cell), C2(small cell), and P1. The P1 crystal form only grows in the presence of 1.4 M DMSO; there are 2 DMSO binding sites per subunit. The structures have been refined at a resolution of 1.83 A, 2.10 A, 2.13 A, and 1.80 A, respectively. In the 4 different spacegroups the TIM subunit can be observed in the context of 7 different crystallographic environments. In the C2 cells, the dimer 2-fold axis coincides with a crystallographic 2-fold axis. The similarities and differences of the 7 subunits are discussed. In 6 subunits the flexible loop (loop 6) is open, whereas in the P2(1)2(1)2(1) cell, the flexible loop of subunit 2 is in an almost closed conformation. The crystal contacts in the 4 different crystal forms are predominantly generated by polar residues in loops. A statistical analysis of the residues involved in crystal contacts shows that, in particular, serines are frequently involved in these interactions; 19% of the exposed serines are involved in crystal contacts.

PubMed: 8061607

Experimental method

X-RAY DIFFRACTION (1.8 Å)