Evidence map›Paper›PMID 28045391›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.

Matthew Wilding, Colin Scott, Janet Newman, Thomas S Peat

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Pathway Driven Target Selection inFrontiers in cellular and infection microbiology · 2022
    Article
  2. 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

4 authors.

Matthew WildingLand and Water, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.
Colin ScottLand and Water, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.
Janet NewmanBiomedical Program, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.
Thomas S PeatBiomedical Program, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionLauric AcidsModels, MolecularPlasmidsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein MultimerizationPseudomonas12-aminododecanoic acidBacterial Proteinsdiamine aminotransferaseLauric AcidsRecombinant ProteinsTransaminases12-aminododecanoic acidaminotransferasesPLP-dependenttransaminase

Identifiers

PMID28045391
PMCPMC5287375

What OpenQuestion holds

Textmetadata
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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.