1H, 13C and 15N resonance assignments of the N-terminal domain of Vta1–Vps60 peptide complex

Yang, Zhuo; Shen, Jie; Zhang, Xu; Vild, C.J.; Lan, Wenxian; Liu, Maili; Xu, Zhaohui; Cao, Chunyang

doi:10.1007/s12104-012-9439-1

Cited by 3 publications

(8 citation statements)

References 10 publications

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“…2E)3334. The helix α4 is much longer in Vta1NTD-Did2 176–204 than that in free Vta1NTD crystal structure, but similar to the observation in NMR structure of Vta1NTD bound to Vps60 128–186 333435. This observation is consistent with our previous secondary structure prediction of free Vta1NTD using the programs CSI38 and TALOS3940 based on the assignments of NMR signals belonging to the backbone atoms of Vta1NTD.…”

Section: Resultssupporting

confidence: 90%

“…The complex Vta1NTD- Did2 176–204 structure shows that the bound Vta1NTD still has two MIT domains, each of them is composed of three α-helices (MIT1: helices α1, α2 and α3; MIT2: helices α5, α6 and α7; respectively), almost similar to those observed in its free state and in its complex with Vps60 128–186 2933343536. The backbone atoms belonging to MIT1 and MIT2 regions of bound Vta1NTD have RMSD values of 1.7 Å and 1.8 Å with those of free Vta1NTD (Fig.…”

Section: Resultsmentioning

confidence: 54%

“…Our NMR structural studies on the interactions between Vta1NTD and Vps60 128–186 revealed that Vps60 128–186 interacted with Vta1NTD in a novel MIT recognition mode, i.e. , through its helices α4′ and α5′ extending over helices 5, 6 and 7 of Vta1NTD MIT2 domain33343536. Previous studies indicated that the C-terminal of Did2, residues 176–204, named as Did2 176–204 in this whole report, as shown in Fig.…”

mentioning

confidence: 57%

“…The linker (64–85aa) between MIT1 and MIT2 domains is well ordered, where residues 66–69 become an α-helix, and residues 73–84 adopt a longer helical structure (here we called it as helix α4) (Fig. 2E)3334. The helix α4 is much longer in Vta1NTD-Did2 176–204 than that in free Vta1NTD crystal structure, but similar to the observation in NMR structure of Vta1NTD bound to Vps60 128–186 333435.…”

Section: Resultsmentioning

confidence: 99%

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NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

Shen

Yang

Wang

et al. 2016

Sci Rep

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As an AAA-ATPase, Vps4 is important for function of multivesicular bodies (MVB) sorting pathway, which involves in cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. The activity of Vps4 is stimulated by the interactions between Vta1 N-terminus (named as Vta1NTD) and Did2 fragment (176–204 aa) (termed as Did2176–204) or Vps60 (128–186 aa) (termed as Vps60128–186). The structural basis of how Vta1NTD binds to Did2176–204 is still unclear. To address this, in this report, the structure of Did2176–204 in complex with Vta1NTD was determined by NMR techniques, demonstrating that Did2176–204 interacts with Vta1NTD through its helix α6′ extending over the 2nd and the 3rd α-helices of Vta1NTD microtubule interacting and transport 1 (MIT1) domain. The residues within Did2176–204 helix α6′ in the interface make up of an amino acid sequence as E192′xxL195′xxR198′L199′xxL202′R203′, identical to type 1 MIT-interacting motif (MIM1) (D/E)xxLxxRLxxL(K/R) of CHMP1A180–196 observed in Vps4-CHMP1A complex structure, indicating that Did2 binds to Vta1NTD through canonical MIM1 interactions. Moreover, the Did2 binding does not result in Vta1NTD significant conformational changes, revealing that Did2, similar to Vps60, enhances Vta1 stimulation of Vps4 ATPase activity in an indirect manner.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 54%

mentioning

confidence: 57%

Section: Resultsmentioning

confidence: 99%

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NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

Shen

Yang

Wang

et al. 2016

Sci Rep

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“…The ESCRT-III subunits Did2 and Vps60 bind to the Vta1 amino-terminal MIT domains (37). Recent structural analysis of these associations revealed that ESCRT-III binding does not effect significant conformational changes within the MIT domains (46,47,55). Removal of the Vta1 MIT domains similarly did not enhance Vta1 stimulation of Vps4 (43).…”

Section: Discussionmentioning

confidence: 99%

Relief of Autoinhibition Enhances Vta1 Activation of Vps4 via the Vps4 Stimulatory Element

Norgan

Davies

Azmi

et al. 2013

Journal of Biological Chemistry

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Background: Vta1 promotes Vps4 ATPase activity and facilitates ESCRT-III stimulation of Vps4. Results: The Vta1 VSE (Vps4 stimulatory element) mediates ESCRT-III-enhanced activation of Vps4 and contributes to Vta1 function in vivo. Conclusion: ESCRT-III binding Vta1 relieves autoinhibition of the VSE to promote activation of Vps4. Significance: These studies identify a novel mechanism whereby ESCRT-III and Vta1 regulate Vps4 activity.

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Structure-based Mechanistic Insights into Terminal Amide Synthase in Nosiheptide-Represented Thiopeptides Biosynthesis

Liu

Guo

Zhang

et al. 2015

Sci Rep

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Nosiheptide is a parent compound of thiopeptide family that exhibit potent activities against various bacterial pathogens. Its C-terminal amide formation is catalyzed by NosA, which is an unusual strategy for maturating certain thiopeptides by processing their precursor peptides featuring a serine extension. We here report the crystal structure of truncated NosA1-111 variant, revealing three key elements, including basic lysine 49 (K49), acidic glutamic acid 101 (E101) and flexible C-terminal loop NosA112-151, are crucial to the catalytic terminal amide formation in nosiheptide biosynthesis. The side-chain of residue K49 and the C-terminal loop fasten the substrate through hydrogen bonds and hydrophobic interactions. The side-chain of residue E101 enhances nucleophilic attack of H2O to the methyl imine intermediate, leading to Cα-N bond cleavage and nosiheptide maturation. The sequence alignment of NosA and its homologs NocA, PbtH, TpdK and BerI, and the enzymatic assay suggest that the mechanistic studies on NosA present an intriguing paradigm about how NosA family members function during thiopeptide biosynthesis.

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1H, 13C and 15N resonance assignments of the N-terminal domain of Vta1–Vps60 peptide complex

Cited by 3 publications

References 10 publications

NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

Relief of Autoinhibition Enhances Vta1 Activation of Vps4 via the Vps4 Stimulatory Element

Structure-based Mechanistic Insights into Terminal Amide Synthase in Nosiheptide-Represented Thiopeptides Biosynthesis

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