Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
about
Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxinStructural characterization of metal binding to a cold-adapted frataxinA New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscSRole of IscX in iron-sulfur cluster biogenesis in Escherichia coliCopper binding in IscA inhibits iron-sulphur cluster assembly in Escherichia coli.Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold proteinCluster and fold stability of E. coli ISC-type ferredoxin.Glycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobinTangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Deletion of the Proposed Iron Chaperones IscA/SufA Results in Accumulation of a Red Intermediate Cysteine Desulfurase IscS in Escherichia coli.The Eukaryotic-Specific ISD11 Is a Complex-Orphan Protein with Ability to Bind the Prokaryotic IscSHuman Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis.Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region.Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes.Hybrid Methods in Iron-Sulfur Cluster Biogenesis.Iron-sulfur cluster biogenesis and trafficking in mitochondria.Understanding the role of dynamics in the iron sulfur cluster molecular machine.The iron-binding CyaY and IscX proteins assist the ISC-catalyzed Fe-S biogenesis in Escherichia coli.A helix-coil transition induced by the metal ion interaction with a grafted iron-binding site of the CyaY protein family.Ferredoxin, in conjunction with NADPH and ferredoxin-NADP reductase, transfers electrons to the IscS/IscU complex to promote iron-sulfur cluster assembly.Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.Molecular chaperones involved in mitochondrial iron-sulfur protein biogenesis.ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin.Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly.Iron-sulfur protein maturation in Helicobacter pylori: identifying a Nfu-type cluster carrier protein and its iron-sulfur protein targets.Fe-S cluster assembly in the supergroup Excavata.NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis
P2860
Q26829187-E97EEBED-BB84-4402-9F00-B435EDA4A22AQ27695962-2CFCF6D1-D624-426A-B4C9-226055C20F70Q27700073-04761036-95C8-4EB9-911D-50EBFC6B5C25Q28828950-24CC94E4-B107-454E-8C67-8DC0FC821177Q33776550-BF0564C0-5BD4-4825-8464-3CB0A7F172DFQ34044012-28D4EF46-8FA3-4149-A6C7-120379E6FC0DQ34430900-5A05E12F-A9B9-4DBE-A8C0-BB17F2E4AC4AQ35050386-5E4D2669-C08F-4315-8D62-512508269D46Q35063787-B6D11A5D-5D8A-47FF-95BA-22C4AC783F16Q35327865-C5CAF9E7-DF8A-428B-BD1B-28E7D8867FADQ35662405-8AA6671B-DFCB-45C4-BB6E-456CD01522B4Q36079884-EAB0466C-33BB-4E78-929D-99A709793531Q37607678-41956FEF-9DDF-448F-A81C-43C193F32E24Q38302783-BC9D6DD9-1242-458C-9FAB-7E0792776835Q39093573-AAF2F152-93F2-4BD8-A526-5BBF48D86A93Q39203982-FC42455B-F172-4F4D-8C39-B6D6E10E69D0Q39374100-1A71362B-B640-43AE-B46A-7C851E14B266Q39635179-D94DE795-2D15-483D-A89A-7D8F13A5C355Q41645273-D6A32676-33B4-45B6-9C8B-7F974ADDD67FQ41657734-3645F117-97C0-42C7-A51B-E59712C846C8Q42588454-5FCF9D98-CF95-47CA-8500-CA02391DE649Q45809936-9B674F34-3466-43D5-9E02-3CBD590609FBQ47159422-2B4A1F20-8323-498D-B5F7-945FCFCCF08DQ47417903-BEA104E1-70D8-4E74-92D2-83406A29AFEEQ50181987-15C88E59-5253-47E4-8C81-DF61794E7492Q52342683-3C4FD451-E803-45DC-8638-079C052D872BQ52689053-2E8D36C3-19B9-47B6-81E1-31D5D023B35AQ55408572-B3FF250D-19CB-4929-8344-1AE16E652BBCQ58778523-A5467DBA-9CCF-496B-97E6-E982D8A0CA3B
P2860
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@ast
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@en
type
label
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@ast
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@en
prefLabel
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@ast
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@en
P2093
P2860
P50
P356
P1476
Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.
@en
P2093
Béatrice Py
Béatrice Roche
Petr V Konarev
Robert Yan
Stephen R Martin
P2860
P304
24777-24787
P356
10.1074/JBC.M113.480327
P407
P577
2013-07-09T00:00:00Z