2v8k

Structure of a Family 2 Pectate Lyase in Complex with Trigalacturonic Acid

spinqualitylabelsall models 2v8k, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v8k is a 1 chain structure with sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: ADA, GTR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A1JSS8_YERE8 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 The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5A, reveals it to be the first prokaryotic protein reported to display the rare (alpha/alpha)(7) barrel fold. In addition to its apo form, we have also determined the structure of a metal-bound form of YePL2A (to 2.0A) and a trigalacturonic acid-bound substrate complex (to 2.1A) Although its fold is rare, the catalytic center of YePL2A can be superimposed with structurally unrelated families, underlining the conserved catalytic amino acid architecture of the beta-elimination mechanism. In addition to its overall structure, YePL2A also has two other unique features: 1) it utilizes a metal atom other than calcium for catalysis, and 2) its Bronstead base is in an alternate conformation and directly interacts with the uronate group of the substrate. A family 2 pectate lyase displays a rare fold and transition metal-assisted beta-elimination.,Abbott DW, Boraston AB J Biol Chem. 2007 Nov 30;282(48):35328-36. Epub 2007 Sep 19. PMID:17881361 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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