5jnp

Publication Abstract from PubMed

The crystallographic structure of a rice cellulose synthase, OsCesA8, plant conserved region (P-CR), one of two unique domains in the catalytic domain of plant CesAs, was solved to 2.4A resolution. Two anti-parallel alpha-helices form a coiled-coil domain linked by a large extended connector loop containing a conserved trio of aromatic residues. The P-CR structure was fit into a molecular envelope for the P-CR domain derived from small-angle X-ray solution scattering data (SAXS). The P-CR structure and molecular envelope, combined with a homology-based chain trace of the CesA8 catalytic core, were modeled into a previously determined CesA8 SAXS molecular envelope to produce a detailed topological model of the CesA8 catalytic domain (CatD). The predicted position for the P-CR domain from the molecular docking models places the P-CR connecting loop into a hydrophobic pocket of the catalytic core, with the coiled-coil aligned near the entrance of the substrate UDP-Glc into the active site. In this configuration the P-CR coiled coil alone is unlikely to regulate substrate access to the active site but it could interact with other domains of CesA, accessory proteins, or other CesA CatDs to control substrate delivery.

Rice Cellulose SynthaseA8 Plant-Conserved Region is a coiled-coil at the catalytic core entrance.,Rushton PS, Olek AT, Makowski L, Badger J, Steussy CN, Carpita NC, Stauffacher CV Plant Physiol. 2016 Nov 22. pii: pp.00739.2016. PMID:27879387^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.