1JTA
Crystal Structure of Pectate Lyase A (C2 form)
Summary for 1JTA
| Entry DOI | 10.2210/pdb1jta/pdb |
| Related | 1JRG |
| Descriptor | pectate lyase A, SULFATE ION (3 entities in total) |
| Functional Keywords | parallel beta helix beta-elimination mechanism, lyase |
| Biological source | Erwinia chrysanthemi |
| Total number of polymer chains | 1 |
| Total formula weight | 38890.67 |
| Authors | Thomas, L.M.,Doan, C.N.,Oliver, R.L.,Yoder, M.D. (deposition date: 2001-08-20, release date: 2002-06-19, Last modification date: 2024-10-16) |
| Primary citation | Thomas, L.M.,Doan, C.N.,Oliver, R.L.,Yoder, M.D. Structure of pectate lyase A: comparison to other isoforms. Acta Crystallogr.,Sect.D, 58:1008-1015, 2002 Cited by PubMed Abstract: Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent beta-elimination mechanism. The crystal structure of pectate lyase A from E. chrysanthemi EC16 has been determined in two crystal forms, monoclinic C2 to 1.8 A and rhombohedral R3 to 2.1 A. The protein structure is compared with two other pectate lyase isoforms from E. chrysanthemi EC16, pectate lyase C and pectate lyase E. Pectate lyase A is unique as it is the only acidic pectate lyase and has end products that are significantly more varied in length in comparison to those of the other four major pectate lyase isozymes. Differences and similarities in polypeptide trace, size and volume of the active-site groove and surface electrostatics are discussed. PubMed: 12037303DOI: 10.1107/S0907444902005851 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
