Evidence map›Paper›PMID 34931065›Full record

ArticleNature chemical biology2022

Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.

Deanna L Mendez, Ethan P Lowder, Dustin E Tillman, Molly C Sutherland, Andrea L Collier, Michael J Rau, James A J Fitzpatrick, Robert G Kranz

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2022. 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
1.4field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 24 citations in OpenAlex.

  1. Heme handling in the system II heme lyase CcsBA from Bacteroides thetaiotaomicron.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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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

8 authors at 1 institution in 1 country.

Deanna L Mendez *Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-0481-4816
Ethan P Lowder *Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0003-1168-2564
Dustin E TillmanDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-7450-0927
Molly C SutherlandDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-7932-5339
Andrea L CollierDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Michael J RauWashington University Center for Cellular Imaging, Washington University School of Medicine, St. Louis, MO, USA.
James A J FitzpatrickWashington University Center for Cellular Imaging, Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-7907-3602
Robert G KranzDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA. kranz@wustl.edu.ORCID http://orcid.org/0000-0002-4309-9413
Washington University in St. Louis · US

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI AIMEE S JAMES · 2001 to 2026
$128.0M
MOLECULAR GENETIC ANALYSES OF CYTOCHROMES C BIOGENESISR01GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1994 to 2019
$6.0M
NCI NIH HHS P30 CA091842NIGMS NIH HHS R01 GM047909
6 · The paper itself

Abstract

Although the individual structures and respiratory functions of cytochromes are well studied, the structural basis for their assembly, including transport of heme for attachment, are unknown. We describe cryo-electron microscopy (cryo-EM) structures of CcsBA, a bifunctional heme transporter and cytochrome c (cyt c) synthase. Models built from the cryo-EM densities show that CcsBA is trapped with heme in two conformations, herein termed the closed and open states. The closed state has heme located solely at a transmembrane (TM) site, with a large periplasmic domain oriented such that access of heme to the cytochrome acceptor is denied. The open conformation contains two heme moieties, one in the TM-heme site and another in an external site (P-heme site). The presence of heme in the periplasmic site at the base of a chamber induces a large conformational shift that exposes the heme for reaction with apocytochrome c (apocyt c). Consistent with these structures, in vivo and in vitro cyt c synthase studies suggest a mechanism for transfer of the periplasmic heme to cytochrome.

Indexed as

Cryoelectron MicroscopyCytochromes cHemeProtein TransportCytochromes cHeme

Identifiers

PMID34931065
PMCPMC8712405
OpenAlexW4200548340

What OpenQuestion holds

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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.