4tt1

Crystal structure of fragment 1600-1733 of HSV1 UL36, native

spinqualitylabelsall models 4tt1, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tt1 is a 2 chain structure with sequence from Human alphaherpesvirus 1 strain 17. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.75Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LTP_HHV11 Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein.[HAMAP-Rule:MF_04044] Publication Abstract from PubMed The tegument of all herpesviruses contains a capsid-bound large protein that is essential for multiple viral processes including capsid transport, decapsidation at the nuclear pore complex, particle assembly and secondary envelopment, through mechanisms that are still incompletely understood. We report here a structural characterization of the central 970 residues of this protein for herpes simplex virus type 1 (HSV-1 UL36, 3164 residues). This large fragment is essentially a 34 nm long monomeric fiber. The crystal structure of its C-terminus shows an elongated, domain-swapped dimer. Modeling and molecular dynamics simulations give a likely molecular organization for the monomeric form and extend our findings to alphaherpesvirinae. Hence, we propose that an essential feature of UL36 is the existence in its central region of a stalk capable of connecting capsid and membrane across the tegument and that the ability to switch between monomeric and dimeric forms may help UL36 fulfill its multiple functions. Insights into Herpesvirus Tegument Organization from Structural Analyses of HSV-1 UL36 Central 970 Residues.,Scrima N, Lepault J, Boulard Y, Pasdeloup D, Bressanelli S, Roche S J Biol Chem. 2015 Feb 12. pii: jbc.M114.612838. PMID:25678705 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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