2XER

Human PatL1 C-terminal domain (loop variant with sulfates)

Summary for 2XER

• Entry DOI: 10.2210/pdb2xer/pdb
• Related: 2XEQ 2XES
• Descriptor: PAT1 HOMOLOG 1, SULFATE ION (3 entities in total)
• Functional Keywords: rna binding protein, mrna decapping, p-bodies
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, P-body: Q86TB9
• Total number of polymer chains: 3
• Total formula weight: 85680.90

Authors

Tritschler, F.,Weichenrieder, O. (deposition date: 2010-05-17, release date: 2010-06-16, Last modification date: 2023-12-20)

Primary citation

Braun, J.E.,Tritschler, F.,Haas, G.,Igreja, C.,Truffault, V.,Weichenrieder, O.,Izaurralde, E.
The C-Terminal Alpha-Alpha Superhelix of Pat is Required for Mrna Decapping in Metazoa.
Embo J., 29:2368-, 2010

PubMed Abstract: Pat proteins regulate the transition of mRNAs from a state that is translationally active to one that is repressed, committing targeted mRNAs to degradation. Pat proteins contain a conserved N-terminal sequence, a proline-rich region, a Mid domain and a C-terminal domain (Pat-C). We show that Pat-C is essential for the interaction with mRNA decapping factors (i.e. DCP2, EDC4 and LSm1-7), whereas the P-rich region and Mid domain have distinct functions in modulating these interactions. DCP2 and EDC4 binding is enhanced by the P-rich region and does not require LSm1-7. LSm1-7 binding is assisted by the Mid domain and is reduced by the P-rich region. Structural analysis revealed that Pat-C folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. This conserved and basic surface is required for RNA, DCP2, EDC4 and LSm1-7 binding. The multiplicity of interactions mediated by Pat-C suggests that certain of these interactions are mutually exclusive and, therefore, that Pat proteins switch decapping partners allowing transitions between sequential steps in the mRNA decapping pathway.

PubMed: 20543818
DOI: 10.1038/EMBOJ.2010.124

Experimental method

X-RAY DIFFRACTION (2.95 Å)