2nt9: Difference between revisions
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|PDB= 2nt9 |SIZE=350|CAPTION= <scene name='initialview01'>2nt9</scene>, resolution 1.90Å | |PDB= 2nt9 |SIZE=350|CAPTION= <scene name='initialview01'>2nt9</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <scene name='pdbligand=M8C:METHYL+ALPHA-D-GALACTOPYRANURONATE'>M8C</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pectinesterase Pectinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.11 3.1.1.11] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pectinesterase Pectinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.11 3.1.1.11] </span> | ||
|GENE= pemA, pem ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | |GENE= pemA, pem ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1qjv|1QJV]], [[2nsp|2NSP]], [[2nst|2NST]], [[2nt6|2NT6]], [[2ntb|2NTB]], [[2ntp|2NTP]], [[2ntq|2NTQ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nt9 OCA], [http://www.ebi.ac.uk/pdbsum/2nt9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nt9 RCSB]</span> | |||
}} | }} | ||
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[[Category: michaelis complex]] | [[Category: michaelis complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:06 2008'' | ||
Revision as of 04:08, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | pemA, pem (Erwinia chrysanthemi) | ||||||
| Activity: | Pectinesterase, with EC number 3.1.1.11 | ||||||
| Related: | 1QJV, 2NSP, 2NST, 2NT6, 2NTB, 2NTP, 2NTQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide IV
OverviewOverview
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.
About this StructureAbout this Structure
2NT9 is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
ReferenceReference
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
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