Evidence map›Paper›PMID 20944213›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.

Constantina Bakolitsa, Abhinav Kumar, Daniel McMullan, S Sri Krishna, Mitchell D Miller, Dennis Carlton, Rafael Najmanovich, Polat Abdubek, Tamara Astakhova, Hsiu Ju Chiu and 33 more

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact, top 86% of its field
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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Journal of bacteriology · 2019
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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

43 authors at 8 institutions in 2 countries.

Constantina BakolitsaStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
Abhinav Kumar
Daniel McMullan
S Sri Krishna
Mitchell D Miller
Dennis Carlton
Rafael Najmanovich
Polat Abdubek
Tamara Astakhova
Hsiu Ju Chiu
Thomas Clayton
Marc C Deller
Lian Duan
Ylva Elias
Julie Feuerhelm
Joanna C Grant
Slawomir K Grzechnik
Gye Won Han
Lukasz Jaroszewski
Kevin K Jin
Heath E Klock
Mark W Knuth
Piotr Kozbial
David Marciano
Andrew T Morse
Edward Nigoghossian
Linda Okach
Silvya Oommachen
Jessica Paulsen
Ron Reyes
Christopher L Rife
Christina V Trout
Henry van den Bedem
Dana Weekes
Aprilfawn White
Qingping Xu
Keith O Hodgson
John Wooley
Marc André Elsliger
Ashley M Deacon
Adam Godzik
Scott A Lesley
Ian A Wilson
Joint Center for Structural Genomics · USSLAC National Accelerator Laboratory · USGenomics Institute of the Novartis Research Foundation · USScripps Research Institute · USUniversity of California, San Diego · USStanford Synchrotron Radiation Lightsource · USSanford Burnham Prebys Medical Discovery Institute · USUniversité de Sherbrooke · CA

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2005 to 2009
$50.6M
JOINT CENTER FOR STRUCTURAL GENOMICSP50GM062411 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WILSON, IAN A · 2000 to 2004
$32.9M
NIGMS NIH HHS P50 GM062411NIGMS NIH HHS P50 GM62411NIGMS NIH HHS U54 GM074898
6 · The paper itself

Abstract

The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded β-sheet wrapped around a single α-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host-pathogen interactions.

Indexed as

Protein FoldingAmino Acid SequenceBacterial ProteinsCrystallography, X-RayGenome, BacterialGlycolipidsModels, MolecularMolecular Sequence DataProtein Structure, QuaternaryProtein Structure, TertiaryPseudomonas aeruginosaBacterial ProteinsGlycolipids

Identifiers

PMID20944213
PMCPMC2954207
OpenAlexW2082658151

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.