5XGG

Crystal Structure C-terminal SH3 domain of Myosin IB from Entamoeba histolytica

Summary for 5XGG

• Entry DOI: 10.2210/pdb5xgg/pdb
• Related: 5XG9
• Descriptor: Unconventional myosin IB, SULFATE ION (3 entities in total)
• Functional Keywords: sh3, myosini, entamoeba histolytica, ehmysh3, contractile protein
• Biological source: Entamoeba histolytica
• Total number of polymer chains: 6
• Total formula weight: 46329.50

Authors

Gautam, G.,Gourinath, S. (deposition date: 2017-04-13, release date: 2017-08-16, Last modification date: 2023-11-22)

Primary citation

Gautam, G.,Rehman, S.A.A.,Pandey, P.,Gourinath, S.
Crystal structure of the PEG-bound SH3 domain of myosin IB from Entamoeba histolytica reveals its mode of ligand recognition
Acta Crystallogr D Struct Biol, 73:672-682, 2017

PubMed Abstract: The versatility in the recognition of various interacting proteins by the SH3 domain drives a variety of cellular functions. Here, the crystal structure of the C-terminal SH3 domain of myosin IB from Entamoeba histolytica (EhMySH3) is reported at a resolution of 1.7 Å in native and PEG-bound states. Comparisons with other structures indicated that the PEG molecules occupy protein-protein interaction pockets similar to those occupied by the peptides in other peptide-bound SH3-domain structures. Also, analysis of the PEG-bound EhMySH3 structure led to the recognition of two additional pockets, apart from the conventional polyproline and specificity pockets, that are important for ligand interaction. Molecular-docking studies combined with various comparisons revealed structural similarity between EhMySH3 and the SH3 domain of β-Pix, and this similarity led to the prediction that EhMySH3 preferentially binds targets containing type II-like PXXP motifs. These studies expand the understanding of the EhMySH3 domain and provide extensive structural knowledge, which is expected to help in predicting the interacting partners which function together with myosin IB during phagocytosis in E. histolytica infections.

PubMed: 28777082
DOI: 10.1107/S2059798317009639

Experimental method

X-RAY DIFFRACTION (1.72 Å)