3KPC

Crystal Structure of the CBS domain pair of protein MJ0100 in complex with 5 -methylthioadenosine and S-adenosyl-L-methionine

Summary for 3KPC

• Entry DOI: 10.2210/pdb3kpc/pdb
• Related: 3KPB 3KPD
• Descriptor: Uncharacterized protein MJ0100, S-ADENOSYLMETHIONINE, 5'-DEOXY-5'-METHYLTHIOADENOSINE, ... (4 entities in total)
• Functional Keywords: cbs domain; s-adenosylmethionine; conformational change, cbs domain, unknown function
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• Total number of polymer chains: 1
• Total formula weight: 14441.81

Authors

Lucas, M.,Oyenarte, I.,Garcia, I.G.,Arribas, E.A.,Encinar, J.A.,Kortazar, D.,Fernandez, J.A.,Mato, J.M.,Martinez-Chantar, M.L.,Martinez-Cruz, L.A. (deposition date: 2009-11-16, release date: 2010-01-12, Last modification date: 2024-02-21)

Primary citation

Lucas, M.,Encinar, J.A.,Arribas, E.A.,Oyenarte, I.,Garcia, I.G.,Kortazar, D.,Fernandez, J.A.,Mato, J.M.,Martinez-Chantar, M.L.,Martinez-Cruz, L.A.
Binding of S-Methyl-5'-Thioadenosine and S-Adenosyl-l-Methionine to Protein MJ0100 Triggers an Open-to-Closed Conformational Change in Its CBS Motif Pair.
J.Mol.Biol., 396:800-820, 2010

PubMed Abstract: Cystathionine beta-synthase (CBS) domains are small motifs that are present in proteins with completely different functions. Several genetic diseases in humans have been associated with mutations in their sequence, which has made them promising targets for rational drug design. The protein MJ0100 from Methanocaldococcus jannaschii includes a DUF39 domain of so far unknown function and a CBS domain pair (Bateman domain) at its C-terminus. This work presents the crystallographic analysis of four different states of the CBS motif pair of MJ0100 in complex with different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5'-thioadenosine (MTA) ligands, providing evidence that ligand-induced conformational reorganization of Bateman domain dimers could be an important regulatory mechanism. These observations are in contrast to what is known from most of the other Bateman domain structures but are supported by recent studies on the magnesium transporter MgtE. Our structures represent the first example of a CBS domain protein complexed with SAM and/or MTA and might provide a structural basis for understanding the molecular mechanisms regulated by SAM upon binding to the C-terminal domain of human CBS, whose structure remains unknown.

PubMed: 20026078
DOI: 10.1016/j.jmb.2009.12.012

Experimental method

X-RAY DIFFRACTION (1.79 Å)