Evidence map›Paper›PMID 16952373›Full record

ArticleJournal of molecular biology2006

PAS domain allostery and light-induced conformational changes in photoactive yellow protein upon I2 intermediate formation, probed with enhanced hydrogen/deuterium exchange mass spectrometry.

Ronald Brudler, Chris R Gessner, Sheng Li, Sammy Tyndall, Elizabeth D Getzoff, Virgil L Woods

Abstract read
In one paragraph

Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Structural basis of SUFU-GLI interaction in human Hedgehog signalling regulation.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. Structural dynamics in DNA damage signaling and repair.Current opinion in structural biology · 2010
    Review
  12. Article
  13. Article
  14. Hydrogen bond dynamics in the active site of photoactive yellow protein.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Conformational studies of the manganese transport regulator (MntR) from Bacillus subtilis using deuterium exchange mass spectrometry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2007
    Article
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

6 authors.

Ronald BrudlerDepartment of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Chris R Gessner
Sheng Li
Sammy Tyndall
Elizabeth D Getzoff
Virgil L Woods

Funding

STRUCTURAL ANALYSIS OF CHROMATICALLY ACTIVE PROTEINSR01GM037684 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D · 1987 to 2009
$3.1M
Enhanced Crystallography of Cancer-Implicated ProteinsR33CA099835 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WOODS, VIRGIL L · 2004 to 2006
$1.8M
DXMS-Facilitated Membrane Protein Construct Design/CancerR21CA118595 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WOODS, VIRGIL L · 2006 to 2007
$420k
Enhanced Crystallography of Cancer-Implicated ProteinsR21CA099835 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI WOODS, VIRGIL L · 2003 to 2003
$142k
NCI NIH HHS CA099835NCI NIH HHS CA118595NCI NIH HHS R21 CA099835NCI NIH HHS R21 CA118595NCI NIH HHS R33 CA099835NIGMS NIH HHS GM37684NIGMS NIH HHS R01 GM037684
6 · The paper itself

Abstract

Photoactive yellow protein (PYP) is a small bacterial photoreceptor that undergoes a light-activated reaction cycle. PYP is also the prototypical Per-Arnt-Sim (PAS) domain. PAS domains, found in diverse multi-domain proteins from bacteria to humans, mediate protein-protein interactions and function as sensors and signal transducers. Here, we investigate conformational and dynamic changes in solution in wild-type PYP upon formation of the long-lived putative signaling intermediate I2 with enhanced hydrogen/deuterium exchange mass spectrometry (DXMS). The DXMS results showed that the central beta-sheet remains stable but specific external protein segments become strongly deprotected. Light-induced disruption of the dark-state hydrogen bonding network in I2 produces increased flexibility and opening of PAS core helices alpha3 and alpha4, releases the beta4-beta5 hairpin, and propagates conformational changes to the central beta-sheet. Surprisingly, the first approximately 10 N-terminal residues, which are essential for fast dark-state recovery from I2, become more protected. By combining the DXMS results with our crystallographic structures, which reveal detailed changes near the chromophore but limited protein conformational change, we propose a mechanism for I2 state formation. This mechanism integrates the results from diverse biophysical studies of PYP, and links an allosteric T to R-state conformational transition to three pathways for signal propagation within the PYP fold. On the basis of the observed changes in PYP plus commonalities shared among PAS domain proteins, we further propose that PAS domains share this conformational mechanism, which explains the versatile signal transduction properties of the structurally conserved PYP/PAS module by framework-encoded allostery.

Indexed as

Deuterium Exchange MeasurementAllosteric SiteBacteriaBacterial ProteinsHumansKineticsLightMass SpectrometryPeptide FragmentsPhotoreceptors, MicrobialProtein Structure, TertiaryBacterial ProteinsPeptide Fragmentsphotoactive yellow protein, BacteriaPhotoreceptors, Microbial

Identifiers

PMID16952373
PMCPMC2575420

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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.