Evidence map›Paper›PMID 25451227›Full record

ArticleFEBS letters2014

Crystal structures of sialyltransferase from Photobacterium damselae.

Nhung Huynh, Yanhong Li, Hai Yu, Shengshu Huang, Kam Lau, Xi Chen, Andrew J Fisher

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  3. Review
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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

7 authors at 1 institution in 1 country.

Nhung HuynhCell Biology Graduate Program, University of California, One Shields Avenue, Davis, CA 95616, USA.
Yanhong LiDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Hai YuDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Shengshu HuangDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Kam LauDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Xi ChenDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA. Electronic address: xiichen@ucdavis.edu.
Andrew J FisherDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA; Department of Molecular and Cellular Biology, University of California, One Shields Avenue, Davis, CA 95616, USA. Electronic address: ajfisher@ucdavis.edu.
University of California, Davis · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Oligosaccharides as antimicrobials and prebioticsR01HD065122 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2010 to 2013
$1.8M
New chemoenzymatic methods for synthesizing complex carbohydratesR01GM094523 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2013 to 2016
$1.2M
NCRR NIH HHS P41 RR001209NICHD NIH HHS R01 HD065122NICHD NIH HHS R01HD065122NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM094523NIGMS NIH HHS R01GM094523
6 · The paper itself

Abstract

Sialyltransferase structures fall into either GT-A or GT-B glycosyltransferase fold. Some sialyltransferases from the Photobacterium genus have been shown to contain an additional N-terminal immunoglobulin (Ig)-like domain. Photobacterium damselae α2-6-sialyltransferase has been used efficiently in enzymatic and chemoenzymatic synthesis of α2-6-linked sialosides. Here we report three crystal structures of this enzyme. Two structures with and without a donor substrate analog CMP-3F(a)Neu5Ac contain an immunoglobulin (Ig)-like domain and adopt the GT-B sialyltransferase fold. The binary structure reveals a non-productive pre-Michaelis complex, which are caused by crystal lattice contacts that prevent the large conformational changes. The third structure lacks the Ig-domain. Comparison of the three structures reveals small inherent flexibility between the two Rossmann-like domains of the GT-B fold.

Indexed as

beta-D-Galactoside alpha 2-6-SialyltransferaseBinding SitesCrystallography, X-RayCytidine Monophosphate N-Acetylneuraminic AcidMetalsModels, MolecularPhotobacteriumProtein Structure, TertiarySialyltransferasesbeta-D-Galactoside alpha 2-6-SialyltransferaseCytidine Monophosphate N-Acetylneuraminic AcidMetalsSialyltransferasesCMP-3F(a)Neu5AcPhotobacterium damselaeProtein crystal structureSialic acidα2–6-Sialyltransferase

Identifiers

PMID25451227
PMCPMC4268365
OpenAlexW1996861551

What OpenQuestion holds

Textmetadata
LicenceTDM
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.