Evidence map›Paper›PMID 19807181›Full record

ArticleJournal of the American Chemical Society2009

Crystal structures of penicillin-binding protein 6 from Escherichia coli.

Yu Chen, Weilie Zhang, Qicun Shi, Dusan Hesek, Mijoon Lee, Shahriar Mobashery, Brian K Shoichet

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Review
  3. Structural Insights for β-Lactam Antibiotics.Biomolecules & therapeutics · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. The putative polysaccharide deacetylase Ba0331: cloning, expression, crystallization and structure determination.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Crystallization and preliminary X-ray crystallographic analysis of PBPD2 from Listeria monocytogenes.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  19. Article
  20. Structural basis for the broad specificity of a new family of amino-acid racemases.Acta crystallographica. Section D, Biological crystallography · 2014
    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

7 authors.

Yu ChenDepartment of Pharmaceutical Chemistry, University of California San Francisco, Byers Hall, Room 508D, 1700 Fourth Street, San Francisco, California 94158-2550, USA.
Weilie Zhang
Qicun Shi
Dusan Hesek
Mijoon Lee
Shahriar Mobashery
Brian K Shoichet

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
Structure, Function and Inhibition of Beta-LactamasesR01GM063815 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SHOICHET, BRIAN K · 2001 to 2013
$2.9M
NIGMS NIH HHS GM61629NIGMS NIH HHS GM63815NIGMS NIH HHS R01 GM061629NIGMS NIH HHS R01 GM063815
6 · The paper itself

Abstract

Penicillin-binding protein 6 (PBP6) is one of the two main DD-carboxypeptidases in Escherichia coli, which are implicated in maturation of bacterial cell wall and formation of cell shape. Here, we report the first X-ray crystal structures of PBP6, capturing its apo state (2.1 A), an acyl-enzyme intermediate with the antibiotic ampicillin (1.8 A), and for the first time for a PBP, a preacylation complex (a "Michaelis complex", determined at 1.8 A) with a peptidoglycan substrate fragment containing the full pentapeptide, NAM-(L-Ala-D-isoGlu-L-Lys-D-Ala-D-Ala). These structures illuminate the molecular interactions essential for ligand recognition and catalysis by DD-carboxypeptidases, and suggest a coupling of conformational flexibility of active site loops to the reaction coordinate. The substrate fragment complex structure, in particular, provides templates for models of cell wall recognition by PBPs, as well as substantiating evidence for the molecular mimicry by beta-lactam antibiotics of the peptidoglycan acyl-D-Ala-D-Ala moiety.

Indexed as

AmpicillinCatalytic DomainCrystallography, X-RayDipeptidasesEscherichia coliEscherichia coli ProteinsModels, MolecularPenicillin-Binding ProteinsPeptide FragmentsStructure-Activity RelationshipAmpicillinDD-carboxypeptidase-endopeptidaseDipeptidasesEscherichia coli ProteinsPenicillin-Binding ProteinsPeptide Fragments

Identifiers

PMID19807181
PMCPMC3697005

What OpenQuestion holds

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Registered trials

None linked

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.