3JXV

Crystal Structure of the 3 FKBP domains of wheat FKBP73

Summary for 3JXV

• Entry DOI: 10.2210/pdb3jxv/pdb
• Descriptor: 70 kDa peptidyl-prolyl isomerase (2 entities in total)
• Functional Keywords: fkbp- binding domain five-stranded anti-parallel beta-sheet and an alpha-helix crossing this sheet, structural genomics, israel structural proteomics center, ispc, calmodulin-binding, isomerase, rotamase, stress response, tpr repeat
• Biological source: Triticum aestivum (wheat)
• Total number of polymer chains: 1
• Total formula weight: 39127.35

Authors

Dym, O.,Breiman, A.,Israel Structural Proteomics Center (ISPC) (deposition date: 2009-09-21, release date: 2010-06-16, Last modification date: 2024-02-21)

Primary citation

Unger, T.,Dym, O.,Albeck, S.,Jacobovitch, Y.,Bernehim, R.,Marom, D.,Pisanty, O.,Breiman, A.
Crystal structure of the three FK506 binding protein domains of wheat FKBP73: evidence for a unique wFK73_2 domain.
J Struct Funct Genomics, 11:113-123, 2010

PubMed Abstract: Here we describe the crystal structure of the N-terminal domain of the FK506-binding protein (FKBP) from wheat (wFKBP73), which is the first structure presenting three FK domains (wFK73_1, wFK73_2 and wFK73_3). The crystal model includes wFK73_2 and wFK73_3 domains and only part of the wFK73_1 domain. The wFK73_1 domain is responsible for binding FK506 and for peptidyl prolyl cis/trans isomerase (PPIase) activity, while the wFK73_2 and wFK73_3 domains lack these activities. A structure-based sequence comparison demonstrated that the absence of a large enough hydrophobic pocket important for PPIase activity, and of the conserved residues necessary for drug binding in the wFK73_2 and wFK73_3 domains explains the lack of these activities in these domains. Sequence and structural comparison between the three wFKBP73 domains suggest that the wFK73_2 domain is the most divergent. A structural comparison of the FK domains of wFKBP73 with other FKBPs containing more than one FK domain, revealed that while the overall architecture of each of the three FK domains displays a typical FKBP fold, their relative arrangement in space is unique and may have important functional implications. We suggest that the existence of FKBPs with three FK domains offers additional interactive options for these plant proteins enlarging the overall regulatory functions of these proteins.

PubMed: 20306145
DOI: 10.1007/s10969-010-9085-8

Experimental method

X-RAY DIFFRACTION (2.08 Å)