4Y7I

Crystal Structure of MTMR8

Summary for 4Y7I

• Entry DOI: 10.2210/pdb4y7i/pdb
• Descriptor: Myotubularin-related protein 8, PHOSPHATE ION (3 entities in total)
• Functional Keywords: mtmr8, myotubularin related protein, phosphoinositid, phosphatase, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus envelope : Q96EF0
• Total number of polymer chains: 2
• Total formula weight: 91091.57

Authors

Yoo, K.,Lee, J.,Son, J.,Shin, W.,Im, D.,Heo, Y.S. (deposition date: 2015-02-15, release date: 2015-07-15, Last modification date: 2024-03-20)

Primary citation

Yoo, K.Y.,Son, J.Y.,Lee, J.U.,Shin, W.,Im, D.W.,Kim, S.J.,Ryu, S.E.,Heo, Y.S.
Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation.
Acta Crystallogr.,Sect.D, 71:1528-1539, 2015

PubMed Abstract: Myotubularin-related proteins are a large family of phosphoinositide phosphatases; their activity, stability and subcellular localization are regulated by dimeric interactions with other members of the family. Here, the crystal structure of the phosphatase domain of MTMR8 is reported. Conformational deviation of the two loops that mediate interaction with the PH-GRAM domain suggests that the PH-GRAM domain interacts differently with the phosphatase domain of each MTMR member. The protein exists as a dimer with twofold symmetry, providing insight into a novel mode of dimerization mediated by the phosphatase domain. Structural comparison and mutation studies suggest that Lys255 of MTMR8 interacts with the substrate diacylglycerol moiety, similar to Lys333 of MTMR2, although the positions of these residues are different. The catalytic activity of the MTMR8 phosphatase domain is inhibited by oxidation and is reversibly reactivated by reduction, suggesting the presence of an oxidation-protective intermediate other than a disulfide bond owing to the absence of a cysteine within a disulfide-bond distance from Cys338.

PubMed: 26143924
DOI: 10.1107/S139900471500927X

Experimental method

X-RAY DIFFRACTION (2.802 Å)