3vcb | pdb_00003vcb

C425S mutant of the C-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus A59

spinqualitylabelsall models 3vcb, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vcb is a 2 chain structure with sequence from Murine coronavirus inf-mhv-a59. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Murine hepatitis virus strain A59 ORF1ab, ORF1A (Murine coronavirus inf-MHV-A59) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q9J3E9_9BETC] Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).[SAAS:SAAS014828_004_014545] Nsp9 is a ssRNA-binding protein (By similarity).[SAAS:SAAS014828_004_001449] Publication Abstract from PubMed BACKGROUND: The replication of coronaviruses takes place on cytoplasmic double membrane vesicles (DMVs) originating in the endoplasmic reticulum (ER). Three trans-membrane non-structural proteins, nsp3, nsp4 and nsp6, are understood to be membrane anchors of the coronavirus replication complex. Nsp4 is localized to the ER membrane when expressed alone but is recruited into the replication complex in infected cells. It is revealed to contain four trans-membrane regions and its N- and C-termini are exposed to the cytosol. METHODOLOGY/PRINCIPAL FINDINGS: We have determined the crystal structures of the C-terminal hydrophilic domain of nsp4 (nsp4C) from MHV strain A59 and a C425S site-directed mutant. The highly conserved 89 amino acid region from T408 to Q496 is shown to possess a new fold. The wild-type (WT) structure features two monomers linked by a Cys425-Cys425 disulfide bond in one asymmetric unit. The monomers are arranged with their N- and C-termini in opposite orientations to form an "open" conformation. Mutation of Cys425 to Ser did not affect the monomer structure, although the mutant dimer adopts strikingly different conformations by crystal packing, with the cross-linked C-termini and parallel N-termini of two monomers forming a "closed" conformation. The WT nsp4C exists as a dimer in solution and can dissociate easily into monomers in a reducing environment. CONCLUSIONS/SIGNIFICANCE: As nsp4C is exposed in the reducing cytosol, the monomer of nsp4C should be physiological. This structure may serve as a basis for further functional studies of nsp4. Crystal structure of the C-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus A59.,Xu X, Lou Z, Ma Y, Chen X, Yang Z, Tong X, Zhao Q, Xu Y, Deng H, Bartlam M, Rao Z PLoS One. 2009 Jul 10;4(7):e6217. PMID:19593433 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase

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