1AIR

PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS

Summary for 1AIR

• Entry DOI: 10.2210/pdb1air/pdb
• Descriptor: PECTATE LYASE C, SULFATE ION (3 entities in total)
• Functional Keywords: pectate cleavage, pectinolyitc activity, trans-elimination
• Biological source: Erwinia chrysanthemi
• Cellular location: Secreted: P11073
• Total number of polymer chains: 1
• Total formula weight: 37925.73

Authors

Lietzke, S.E.,Scavetta, R.D.,Yoder, M.D.,Jurnak, F.A. (deposition date: 1997-04-24, release date: 1997-06-16, Last modification date: 2024-10-30)

Primary citation

Lietzke, S.E.,Scavetta, R.D.,Yoder, M.D.,Jurnak, F.
The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution.
Plant Physiol., 111:73-92, 1996

PubMed Abstract: The crystal structure of pectate lyase E (PelE; EC 4.2.2.2) from the enterobacteria Erwinia chrysanthemi has been refined by molecular dynamics techniques to a resolution of 2.2 A and an R factor (an agreement factor between observed structure factor amplitudes) of 16.1%. The final model consists of all 355 amino acids and 157 water molecules. The root-mean-square deviation from ideality is 0.009 A for bond lengths and 1.721[deg] for bond angles. The structure of PelE bound to a lanthanum ion, which inhibits the enzymatic activity, has also been refined and compared to the metal-free protein. In addition, the structures of pectate lyase C (PelC) in the presence and absence of a lutetium ion have been refined further using an improved algorithm for identifying waters and other solvent molecules. The two putative active site regions of PelE have been compared to those in the refined structure of PelC. The analysis of the atomic details of PelE and PelC in the presence and absence of lanthanide ions provides insight into the enzymatic mechanism of pectate lyases.

PubMed: 12226275

Experimental method

X-RAY DIFFRACTION (2.2 Å)