The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).

Plant physiology ·Vol. 107 ·No. 2 ·1995-02-00 ·Pages 349-364

Yoder MD, Jurnak F

Abstract

The crystal structure of pectate lyase C (EC 4.2.2.2) from the enterobacterium Erwinia chrysanthemi (PelC) has been refined by molecular dynamics techniques to a resolution of 2.2 A to an R factor of 17.97%. The final model consists of 352 of the total 353 amino acids and 114 solvent molecules. The root-mean-square deviation from ideality is 0.009 A for bond lengths and 1.768[deg] for bond angles. The structure of PelC bound to the lanthanide ion lutetium, used as a calcium analog, has also been refined. Lutetium inhibits the enzymatic activity of the protein, and in the PelC-lutetium structure, the ion binds in the putative calcium-binding site. Five side-chain atoms form ligands to the lutetium ion. An analysis of the atomic-level model of the two protein structures reveals possible implications for the enzymatic mechanism of the enzyme.

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Yoder M. D.

School of Biological Sciences, Division of Cell Biology and Biophysics, University of Missouri, Kansas City, Missouri 64110 (M.D.Y.).

Jurnak F.

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Article Info

Journal

Plant physiology

Abbr.

Plant Physiol

ISSN

1532-2548

DOI

10.1104/pp.107.2.349

Published

1995-02-00

Pages

349-364

Language

English

Region

United States

NLM ID

0401224

PMCID

PMC157135

External Links

PubMed source DOI: 10.1104/pp.107.2.349 PMC Full Text View journal details

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The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).

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