Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZSQ

Crystal Structure of MTMR2 in complex with phosphatidylinositol 3-phosphate

Summary for 1ZSQ
Entry DOI10.2210/pdb1zsq/pdb
DescriptorMyotubularin-related protein 2, 1,2-ETHANEDIOL, 2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL)OXY]METHYL}ETHYL BUTANOATE, ... (4 entities in total)
Functional Keywordsprotein-phospholipid complex, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q13614
Total number of polymer chains1
Total formula weight61907.05
Authors
Begley, M.J.,Taylor, G.S.,Brock, M.A.,Ghosh, P.,Woods, V.L.,Dixon, J.E. (deposition date: 2005-05-25, release date: 2006-01-31, Last modification date: 2023-08-23)
Primary citationBegley, M.J.,Taylor, G.S.,Brock, M.A.,Ghosh, P.,Woods, V.L.,Dixon, J.E.
Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase
Proc.Natl.Acad.Sci.Usa, 103:927-932, 2006
Cited by
PubMed Abstract: Myotubularins, a large family of catalytically active and inactive proteins, belong to a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as physiological substrates. Here, by integrating crystallographic and deuterium-exchange mass spectrometry studies of human myotubularin-related protein-2 (MTMR2) in complex with phosphoinositides, we define the molecular basis for this unique substrate specificity. Phosphoinositide substrates bind in a pocket located on a positively charged face of the protein, suggesting an electrostatic mechanism for membrane targeting. A flexible, hydrophobic helix makes extensive interactions with the diacylglycerol moieties of substrates, explaining the specificity for membrane-bound phosphoinositides. An extensive H-bonding network and charge-charge interactions within the active site pocket determine phosphoinositide headgroup specificity. The conservation of these specificity determinants within the active, but not the inactive, myotubularins provides insight into the functional differences between the active and inactive members.
PubMed: 16410353
DOI: 10.1073/pnas.0510006103
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.82 Å)
Structure validation

239492

数据于2025-07-30公开中

PDB statisticsPDBj update infoContact PDBjnumon