6RIY

Crystal structure of MchDnaB-1 intein (N145AA)

Summary for 6RIY

• Entry DOI: 10.2210/pdb6riy/pdb
• Descriptor: Replicative DNA helicase, CHLORIDE ION (3 entities in total)
• Functional Keywords: intein, protein-splicing, splicing, hydrolase
• Biological source: Mycobacterium chimaera
• Total number of polymer chains: 2
• Total formula weight: 30225.60

Authors

Beyer, H.M.,Lountos, G.T.,Mikula, M.K.,Wlodawer, A.,Iwai, H. (deposition date: 2019-04-25, release date: 2020-05-13, Last modification date: 2024-01-24)

Primary citation

Beyer, H.M.,Virtanen, S.I.,Aranko, A.S.,Mikula, K.M.,Lountos, G.T.,Wlodawer, A.,Ollila, O.H.S.,Iwai, H.
The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms.
Int J Mol Sci, 21:-, 2020

PubMed Abstract: Protein splicing catalyzed by inteins utilizes many different combinations of amino-acid types at active sites. Inteins have been classified into three classes based on their characteristic sequences. We investigated the structural basis of the protein splicing mechanism of class 3 inteins by determining crystal structures of variants of a class 3 intein from and molecular dynamics simulations, which suggested that the class 3 intein utilizes a different splicing mechanism from that of class 1 and 2 inteins. The class 3 intein uses a bond cleavage strategy reminiscent of proteases but share the same Hedgehog/INTein (HINT) fold of other intein classes. Engineering of class 3 inteins from a class 1 intein indicated that a class 3 intein would unlikely evolve directly from a class 1 or 2 intein. The HINT fold appears as structural and functional solution for -peptidyl and -esterification reactions commonly exploited by diverse mechanisms using different combinations of amino-acid types for the active-site residues.

PubMed: 33171880
DOI: 10.3390/ijms21218367

Experimental method

X-RAY DIFFRACTION (1.63 Å)