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Rice Cellulose SynthaseA8 Plant-Conserved Region Is a Coiled-Coil at the Catalytic Core Entrance
Phillip S Rushton1,2,3, Anna T Olek1,2,3, Lee Makowski1,2,3
1Department of Biological Sciences (P.S.R., C.N.S., N.C.C., C.V.S.), Department of Botany and Plant Pathology (A.T.O., N.C.C.), Bindley Bioscience Center (N.C.C., C.V.S.), and Purdue Center for Cancer Research (C.V.S.), Purdue University, West Lafayette, Indiana 47907.
Plant Physiology
|November 24, 2016
Summary
Researchers determined the structure of a rice cellulose synthase (OsCesA8) plant-conserved region. This region
Area of Science:
- Plant biology
- Biochemistry
- Structural biology
Background:
- Cellulose synthases (CesAs) are crucial enzymes for plant cell wall biosynthesis.
- The plant-conserved region (P-CR) is a unique domain within the catalytic domain of CesAs, but its structural role remains unclear.
Purpose of the Study:
- To elucidate the three-dimensional structure of the rice OsCesA8 P-CR domain.
- To develop a detailed topological model of the OsCesA8 catalytic domain incorporating the P-CR structure.
Main Methods:
- X-ray crystallography was used to solve the structure of the OsCesA8 P-CR domain to 2.4 Å resolution.
- Small-angle X-ray scattering (SAXS) data provided a molecular envelope for the P-CR domain.
- Homology modeling and molecular docking were employed to integrate the P-CR structure into the CesA8 catalytic core model.
Main Results:
- The OsCesA8 P-CR structure revealed a coiled-coil domain formed by two antiparallel α-helices, linked by a loop with conserved aromatic residues.
- Molecular docking predicted the P-CR coiled-coil to be positioned near the UDP-glucose active site entrance within the catalytic core.
- The P-CR connector loop was modeled into a hydrophobic pocket of the catalytic core.
Conclusions:
- The P-CR domain's structure and predicted localization provide insights into the OsCesA8 catalytic domain architecture.
- While the P-CR coiled-coil may not directly regulate substrate access, it could play a role in interactions with other protein components to control cellulose synthesis.
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