5OXX

Crystal structure of NeqN/NeqC complex from Nanoarcheaum equitans at 1.7A

Summary for 5OXX

• Entry DOI: 10.2210/pdb5oxx/pdb
• Descriptor: NEQ068, NEQ528 (3 entities in total)
• Functional Keywords: intein complex, splicing
• Biological source: Nanoarchaeum equitans (strain Kin4-M); More
• Total number of polymer chains: 2
• Total formula weight: 16141.31

Authors

Aparicio, D.,Perez-Luque, R.,Ribo, M.,Fita, I. (deposition date: 2017-09-07, release date: 2018-10-10, Last modification date: 2024-01-17)

Primary citation

Gordo, V.,Aparicio, D.,Perez-Luque, R.,Benito, A.,Vilanova, M.,Uson, I.,Fita, I.,Ribo, M.
Structural Insights into Subunits Assembly and the Oxyester Splicing Mechanism of Neq pol Split Intein.
Cell Chem Biol, 25:871-879.e2, 2018

PubMed Abstract: Split inteins are expressed as two separated subunits (N-intein and C-intein) fused to the corresponding exteins. The specific association of both intein subunits precedes protein splicing, which results in excision of the intein subunits and in ligation, by a peptide bond, of the concomitant exteins. Catalytically active intein precursors are typically too reactive for crystallization or even isolation. Neq pol is the trans-intein of the B-type DNA polymerase I split gene from hyperthermophile Nanoarchaeum equitans. We have determined the crystal structures of both the isolated NeqN and the complex of NeqN and NeqC subunits carrying the wild-type sequences, including the essential catalytic residues Ser1 and Thr+1, in addition to seven and three residues of the N- and C-exteins, respectively. These structures provide detailed information on the unique oxyester chemistry of the splicing mechanism of Neq pol and of the extensive rearrangements that occur in NeqN during the association step.

PubMed: 29754955
DOI: 10.1016/j.chembiol.2018.04.008

Experimental method

X-RAY DIFFRACTION (1.74 Å)