6K7F

Crystal structure of MBPholo-Tim21 fusion protein with a 17-residue helical linker

Summary for 6K7F

Entry DOI	10.2210/pdb6k7f/pdb
Related PRD ID	PRD_900001
Descriptor	Maltose/maltodextrin-binding periplasmic protein,Mitochondrial import inner membrane translocase subunit TIM21, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
Functional Keywords	mbp, tim21, fusion protein, helical linker, translocase, sugar binding protein
Biological source	Escherichia coli (strain K12) More
Total number of polymer chains	1
Total formula weight	55990.56
Authors	Bala, S.,Shimada, A.,Kohda, D. (deposition date: 2019-06-07, release date: 2019-09-18, Last modification date: 2023-11-22)
Primary citation	Bala, S.,Shinya, S.,Srivastava, A.,Ishikawa, M.,Shimada, A.,Kobayashi, N.,Kojima, C.,Tama, F.,Miyashita, O.,Kohda, D. Crystal contact-free conformation of an intrinsically flexible loop in protein crystal: Tim21 as the case study. Biochim Biophys Acta Gen Subj, 1864:129418-129418, 2020 Cited by PubMed Abstract: In protein crystals, flexible loops are frequently deformed by crystal contacts, whereas in solution, the large motions result in the poor convergence of such flexible loops in NMR structure determinations. We need an experimental technique to characterize the structural and dynamic properties of intrinsically flexible loops of protein molecules. PubMed: 31449839 DOI: 10.1016/j.bbagen.2019.129418 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation