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4tt0

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Revision as of 01:24, 19 January 2017

Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M potassium iodide

Structural highlights

4tt0 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DEN_HHV11] Deneddylase that deregulates the host cell cycle S phase to create a favorable environment allowing efficient viral genome replication. Interacts with and deneddylates host cullins including CUL1 and CUL4A, thereby reducing their E3 ubiquitin ligase activity. Inhibition of cullins leads to the stabilization of cullin-RING ligase substrates such as host CDN1A/p21, CDKN1B/p27kip and CDC25A, preventing S phase progression. Additionally, acts as a deubiquitinase and cleaves both 'Lys-48' and 'Lys-63'-linked ubiquitin chains (By similarity).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Scrima N, Lepault J, Boulard Y, Pasdeloup D, Bressanelli S, Roche S. Insights into Herpesvirus Tegument Organization from Structural Analyses of HSV-1 UL36 Central 970 Residues. J Biol Chem. 2015 Feb 12. pii: jbc.M114.612838. PMID:25678705 doi:http://dx.doi.org/10.1074/jbc.M114.612838

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4tt0"

Categories: Bressanelli, S | Roche, S | Scrima, N | Fibrous protein tegument protein | Hydrolase

@@ Line 1: / Line 1: @@
 ==Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M potassium iodide==
 <StructureSection load='4tt0' size='340' side='right' caption='[[4tt0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4tt0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TT0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TT0 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tt0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tt0 RCSB], [http://www.ebi.ac.uk/pdbsum/4tt0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tt0 OCA], [http://pdbe.org/4tt0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tt0 RCSB], [http://www.ebi.ac.uk/pdbsum/4tt0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tt0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4tt0" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4tt0

From Proteopedia

Revision as of 01:24, 19 January 2017

Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M potassium iodide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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