Results 21 to 30 of about 213,829 (198)

Structures of the CcmABCD heme release complex at multiple states

Nature Communications, 2022
Bacterial ABC transporter complex CcmABCD, a part of cytochrome c maturation system, transfers heme from one binding partner (CcmC) to another (CcmE). Here authors describe high resolution cryo-EM structures of CcmABCD in multiple states and propose a ...
Jiao Li, Wan Zheng, Ming Gu, Long Han, Yanmei Luo, Koukou Yu, Mengxin Sun, Yuliang Zong, Xiuxiu Ma, Bing Liu, Ethan P. Lowder, Deanna L. Mendez, Robert G. Kranz, Kai Zhang, Jiapeng Zhu   +14 more
doaj   +1 more source

The CcmC:Heme:CcmE Complex in Heme Trafficking and Cytochrome c Biosynthesis [PDF]

Journal of Molecular Biology, 2010
A superfamily of integral membrane proteins is characterized by a conserved tryptophan-rich region (called the WWD domain) in an external loop at the inner membrane surface. The three major members of this family (CcmC, CcmF, and CcsBA) are each involved in cytochrome c biosynthesis, yet the function of the WWD domain is unknown.
Cynthia, Richard-Fogal, Robert G, Kranz
openaire   +2 more sources

Structural basis of membrane machines that traffick and attach heme to cytochromes

Journal of Biological Chemistry, 2023
We evaluate cryoEM and crystal structures of two molecular machines that traffick heme and attach it to cytochrome c (cyt c), the second activity performed by a cyt c synthase. These integral membrane proteins, CcsBA and CcmF/H, both covalently attach heme to cyt c, but carry it out via different mechanisms.
Jonathan Q. Huynh, Ethan P. Lowder, Robert G. Kranz   +2 more
openaire   +2 more sources

Identification of the Mitochondrial Heme Metabolism Complex. [PDF]

PLoS ONE, 2015
Heme is an essential cofactor for most organisms and all metazoans. While the individual enzymes involved in synthesis and utilization of heme are fairly well known, less is known about the intracellular trafficking of porphyrins and heme, or regulation ...
Amy E Medlock, Mesafint T Shiferaw, Jason R Marcero, Ajay A Vashisht, James A Wohlschlegel, John D Phillips, Harry A Dailey   +6 more
doaj   +1 more source

Structure-Function Analysis of the Bifunctional CcsBA Heme Exporter and Cytochrome c Synthetase

mBio, 2018
Although intracellular heme trafficking must occur for heme protein assembly, only a few heme transporters have been unequivocally discovered and nothing is known about their structure or mechanisms.
Molly C. Sutherland, Nathan L. Tran, Dustin E. Tillman, Joshua M. Jarodsky, Jason Yuan, Robert G. Kranz   +5 more
doaj   +1 more source

Heme Oxygenase-1 Regulates Myeloid Cell Trafficking in AKI [PDF]

Journal of the American Society of Nephrology, 2015
Renal ischemia-reperfusion injury is mediated by a complex cascade of events, including the immune response, that occur secondary to injury to renal epithelial cells. We tested the hypothesis that heme oxygenase-1 (HO-1) expression, which is protective in ischemia-reperfusion injury, regulates trafficking of myeloid-derived immune cells in the kidney ...
Travis D, Hull, Ahmed I, Kamal, Ravindra, Boddu, Subhashini, Bolisetty, Lingling, Guo, Cornelia C, Tisher, Sunil, Rangarajan, Bo, Chen, Lisa M, Curtis, James F, George, Anupam, Agarwal   +10 more
openaire   +2 more sources

Genetic screens reveal CCDC115 as a modulator of erythroid iron and heme trafficking [PDF]

American Journal of Hematology, 2020
AbstractTransferrin‐bound iron (TBI), the physiological circulating iron form, is acquired by cells through the transferrin receptor (TfR1) by endocytosis. In erythroid cells, most of the acquired iron is incorporated into heme in the mitochondria. Cellular trafficking of heme is indispensable for erythropoiesis and many other essential biological ...
Amin Sobh, Alex Loguinov, Jie Zhou, Supak Jenkitkasemwong, Rola Zeidan, Nader El Ahmadie, Abderrahmane Tagmount, Mitchell Knutson, Paula G. Fraenkel, Christopher D. Vulpe   +9 more
openaire   +2 more sources

Heme degrading protein HemS is involved in oxidative stress response of Bartonella henselae. [PDF]

PLoS ONE, 2012
Bartonellae are hemotropic bacteria, agents of emerging zoonoses. These bacteria are heme auxotroph Alphaproteobacteria which must import heme for supporting their growth, as they cannot synthesize it.
MaFeng Liu, Henri-Jean Boulouis, Francis Biville   +2 more
doaj   +1 more source

Down the Iron Path: Mitochondrial Iron Homeostasis and Beyond

Cells, 2021
Cellular iron homeostasis and mitochondrial iron homeostasis are interdependent. Mitochondria must import iron to form iron–sulfur clusters and heme, and to incorporate these cofactors along with iron ions into mitochondrial proteins that support ...
Jonathan V. Dietz, Jennifer L. Fox, Oleh Khalimonchuk   +2 more
doaj   +1 more source

Biosynthesis and trafficking of heme o and heme a: new structural insights and their implications for reaction mechanisms and prenylated heme transfer

Critical Reviews in Biochemistry and Molecular Biology, 2021
Aerobic respiration is a key energy-producing pathway in many prokaryotes and virtually all eukaryotes. The final step of aerobic respiration is most commonly catalyzed by heme-copper oxidases embedded in the cytoplasmic or mitochondrial membrane. The majority of these terminal oxidases contain a prenylated heme (typically heme a or occasionally heme o)
Elise D. Rivett, Lim Heo, Michael Feig, Eric L. Hegg   +3 more
openaire   +3 more sources