2nt6

Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide III

spinqualitylabelsall models 2nt6, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nt6 is a 2 chain structure with sequence from Dicd3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADA, M8C Related: 1qjv, 2nsp, 2nst, 2nt9, 2ntb, 2ntp, 2ntq Gene: pemA, pem (DICD3) Activity: Hydrolase, with EC number 3.1.1.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PMEA_DICD3] Involved in maceration and soft-rotting of plant tissue. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We provide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the essential first step in bacterial invasion of plant tissues. The complexes formed in the crystal using specifically methylated pectins, together with kinetic measurements of directed mutants, provide clear insights at atomic resolution into the specificity and the processive action of the Erwinia chrysanthemi enzyme. Product complexes provide additional snapshots along the reaction coordinate. We previously revealed that PME is a novel aspartic-esterase possessing parallel beta-helix architecture and now show that the two conserved aspartates are the nucleophile and general acid-base in the mechanism, respectively. Other conserved residues at the catalytic centre are shown to be essential for substrate binding or transition state stabilisation. The preferential binding of methylated sugar residues upstream of the catalytic site, and demethylated residues downstream, drives the enzyme along the pectin molecule and accounts for the sequential pattern of demethylation produced by both bacterial and plant PMEs. Molecular basis of the activity of the phytopathogen pectin methylesterase.,Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW EMBO J. 2007 Sep 5;26(17):3879-87. Epub 2007 Aug 23. PMID:17717531 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methylesterase 3D structures

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