2V8K
Structure of a Family 2 Pectate Lyase in Complex with Trigalacturonic Acid
Summary for 2V8K
| Entry DOI | 10.2210/pdb2v8k/pdb |
| Related | 2V8I 2V8J |
| Descriptor | PECTATE LYASE, beta-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid (3 entities in total) |
| Functional Keywords | lyase, pectate lyase, beta-elimination, pectin degradation |
| Biological source | YERSINIA ENTEROCOLITICA |
| Total number of polymer chains | 1 |
| Total formula weight | 61803.88 |
| Authors | Abbott, D.W.,Boraston, A.B. (deposition date: 2007-08-08, release date: 2007-09-18, Last modification date: 2024-05-08) |
| Primary citation | Abbott, D.W.,Boraston, A.B. A Family 2 Pectate Lyase Displays a Rare Fold and Transition Metal-Assisted Beta-Elimination. J.Biol.Chem., 282:35328-, 2007 Cited by PubMed Abstract: 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 Brønstead base is in an alternate conformation and directly interacts with the uronate group of the substrate. PubMed: 17881361DOI: 10.1074/JBC.M705511200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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