4TMY

CHEY FROM THERMOTOGA MARITIMA (MG-IV)

Summary for 4TMY

• Entry DOI: 10.2210/pdb4tmy/pdb
• Descriptor: CHEY PROTEIN, MAGNESIUM ION (2 entities in total)
• Functional Keywords: chemotaxis, phosphoryl transfer, signal transduction, magnesium binding
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm: Q56312
• Total number of polymer chains: 2
• Total formula weight: 26518.12

Authors

Usher, K.C.,De La Cruz, A.,Dahlquist, F.W.,Remington, S.J. (deposition date: 1997-06-06, release date: 1997-12-03, Last modification date: 2024-05-22)

Primary citation

Usher, K.C.,de la Cruz, A.F.,Dahlquist, F.W.,Swanson, R.V.,Simon, M.I.,Remington, S.J.
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.
Protein Sci., 7:403-412, 1998

PubMed Abstract: The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.

PubMed: 9521117

Experimental method

X-RAY DIFFRACTION (2.8 Å)