Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
about
Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)Active site remodelling accompanies thioester bond formation in the SUMO E1Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimerA unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologsEvidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humansStructures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathwaysStructure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesisProkaryotic ubiquitin-like protein modificationNMR structure of conserved eukaryotic protein ZK652.3 from C. elegans: a ubiquitin-like foldStructural studies of molybdopterin synthase provide insights into its catalytic mechanismInsights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structureBiochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobAThe SoxYZ complex carries sulfur cycle intermediates on a peptide swinging armSequence and structure evolved separately in a ribosomal ubiquitin variantStructural Dissection of a Gating Mechanism Preventing Misactivation of Ubiquitin by NEDD8’s E1 † ‡Crystal Structure of a Sulfur Carrier Protein Complex Found in the Cysteine Biosynthetic Pathway of Mycobacterium tuberculosis † ‡How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibioticCrystal Structure of the Human Ubiquitin-activating Enzyme 5 (UBA5) Bound to ATP: MECHANISTIC INSIGHTS INTO A MINIMALISTIC E1 ENZYMECrystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organismsAtg8 Transfer from Atg7 to Atg3: A Distinctive E1-E2 Architecture and Mechanism in the Autophagy PathwayInsights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8Structure of the ubiquitin-activating enzyme loaded with two ubiquitin moleculesExpression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1)Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactorCrystal structure of a fragment of mouse ubiquitin-activating enzymePleiotropic effects of ATP.Mg2+ binding in the catalytic cycle of ubiquitin-activating enzymePerilous journey: a tour of the ubiquitin-proteasome systemFunctional analysis of molybdopterin biosynthesis in mycobacteria identifies a fused molybdopterin synthase in Mycobacterium tuberculosisKinetic and structural insights into the mechanism of AMPylation by VopS Fic domainThe crystal structure and small-angle X-ray analysis of CsdL/TcdA reveal a new tRNA binding motif in the MoeB/E1 superfamilyThe dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrierUrm1 at the crossroad of modifications. 'Protein Modifications: Beyond the Usual Suspects' Review SeriesSolution structure of Urm1 and its implications for the origin of protein modifiersUbiquitin and ubiquitin-like proteins as multifunctional signalsThe prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains.Natural history of the E1-like superfamily: implication for adenylation, sulfur transfer, and ubiquitin conjugation.Isolation and sequence of an interferon-tau-inducible, pregnancy- and bovine interferon-stimulated gene product 15 (ISG15)-specific, bovine ubiquitin-activating E1-like (UBE1L) enzyme.
P2860
Q21283989-30AD5B9F-7A03-4294-902D-01F55E20FE5EQ24299970-BE51068D-E77D-44E3-8511-F4C6DADB52F3Q24301571-77056C7D-C034-4CB6-BB59-418D8B6B73CFQ24303664-E74C8D0B-9466-4879-9C32-4DCE7FE22206Q24303892-AC668925-4F86-476B-85F2-0125411F7C6BQ24336143-2AF4B614-112E-44C2-96BA-1D2E9BDD7885Q24338548-5BBE6695-2215-40AA-8851-025CC76860E1Q24647626-ADBE4017-2B31-4EC0-973F-D994317539B6Q24653002-6388A997-3708-436A-9D1A-43E0386930EFQ26998484-EE48501B-86C3-4856-9A46-24D2BEFFB52CQ27639587-586976EE-2548-4D66-BBF3-69B4E583E3E7Q27640444-DCF8B949-9ED5-4714-BC7D-B52FCCBE9B89Q27640736-7C99B238-69F0-4A87-B095-EC675955D6F8Q27640918-FC59EEA2-3D3B-4CAB-A40D-DCB45E1E0B3BQ27641091-D7E6F16F-BD75-4ADC-AD9E-95FA321210D8Q27644861-ED4A2AFB-EC2A-4F83-A238-C9E6D4C888D8Q27646472-3B1EF38C-4C11-44F0-8970-D362D3B152F3Q27651318-2D63BD20-943F-4CEF-B825-B32D9246D276Q27651982-6425BA16-C011-4041-AC74-B02E28FE89E9Q27655732-4D1794FA-E4E0-4AD5-9ED9-7C98D01F4CD6Q27660424-C14E2A81-8FCD-4277-BDBA-0C4B1EFB0CA6Q27666470-AE73D715-138D-4188-AAC3-84E101C27CAAQ27675398-6A9445F0-9809-494A-84EB-EC67C21D18A5Q27675408-6A0A603D-EDDF-466C-86D1-69608A572218Q27690199-162302DA-9E0B-438F-A36D-CB0E77E71E32Q27695600-E527A9F8-5D15-4165-91C2-D46150997B91Q27700216-ADE08F00-48B8-40F5-A55A-F945C172F1B2Q28240284-A9222B25-6F7D-446D-95E9-39BF6F492F0BQ28305802-64E63F4E-A8FB-4DE2-ADDC-C31BA7A477B7Q28306492-652C14AD-7976-4E5C-8C42-DCC2BA7C9BDEQ28486812-027D7C23-B27D-43AF-89F9-55C3C979DCDBQ28492217-0BEDF44D-A42C-41F7-AEBD-F3ABD8C5D77BQ28546621-F9B9FF1A-406D-4886-89B0-91ED2BFB3277Q28602413-1224A741-CD80-46CF-8282-B59DCD0ADEEBQ28756158-24BE5D78-C5B4-466D-A388-B1258C1FAA50Q28768369-1068D13E-14B7-4C9A-9DBA-D2BD80605420Q30014838-7C92C2CB-0443-4B59-BF7B-4505A7587E34Q30820062-B25D019D-1053-455D-8E1D-753E1A7662AEQ30855071-1623AF43-C68B-4990-A70C-4B605E67D14BQ31114732-9B28EF74-2C9E-4380-8BA9-E08678F775B4
P2860
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@ast
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@en
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@nl
type
label
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@ast
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@en
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@nl
prefLabel
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@ast
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@en
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@nl
P2093
P2860
P356
P1433
P1476
Mechanism of ubiquitin activat ...... a bacterial MoeB-MoaD complex
@en
P2093
K V Rajagopalan
M M Wuebbens
P2860
P2888
P356
10.1038/35104586
P407
P577
2001-11-15T00:00:00Z
P5875
P6179
1013748717