Evidence map›Paper›PMID 27879387›Full record

ArticlePlant physiology2017

Rice Cellulose SynthaseA8 Plant-Conserved Region Is a Coiled-Coil at the Catalytic Core Entrance.

Phillip S Rushton, Anna T Olek, Lee Makowski, John Badger, C Nicklaus Steussy, Nicholas C Carpita, Cynthia V Stauffacher

Abstract read
In one paragraph

Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Structure ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Cellulose synthase complex organization and cellulose microfibril structure.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2018
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Phillip S RushtonDepartment 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.
Anna T OlekDepartment 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.
Lee MakowskiDepartment 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.
John BadgerDepartment 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.
C Nicklaus SteussyDepartment 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.ORCID 0000-0002-0482-3165
Nicholas C CarpitaDepartment 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.ORCID 0000-0003-0770-314X
Cynthia V StauffacherDepartment 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; cstauffa@purdue.edu.ORCID 0000-0002-3081-6903

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
NCI NIH HHS P30 CA023168NIGMS NIH HHS P41 GM103622
6 · The paper itself

Abstract

The crystallographic structure of a rice (Oryza sativa) cellulose synthase, OsCesA8, plant-conserved region (P-CR), one of two unique domains in the catalytic domain of plant CesAs, was solved to 2.4 Å resolution. Two antiparallel α-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 scattering data. 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 small-angle X-ray scattering molecular envelope to produce a detailed topological model of the CesA8 catalytic domain. The predicted position for the P-CR domain from the molecular docking models places the P-CR connector loop into a hydrophobic pocket of the catalytic core, with the coiled-coil aligned near the entrance of the substrate UDP-glucose 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 catalytic domains to control substrate delivery.

Indexed as

Catalytic DomainCrystallography, X-RayGlucosyltransferasesModels, MolecularMolecular Docking SimulationOryzaPlant ProteinsProtein ConformationScattering, Small AngleX-Ray Diffractioncellulose synthaseGlucosyltransferasesPlant Proteins

Identifiers

PMID27879387
PMCPMC5210708

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.