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==Crystal structure of human G3BP1 in complex with Semliki Forest Virus nsP3-25 comprising two FGDF motives==
==Crystal structure of human G3BP1 in complex with Semliki Forest Virus nsP3-25 comprising two FGDF motives==
<StructureSection load='5fw5' size='340' side='right' caption='[[5fw5]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
<StructureSection load='5fw5' size='340' side='right'caption='[[5fw5]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5fw5]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FW5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5fw5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Semliki_Forest_virus Semliki Forest virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FW5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</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=5fw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fw5 OCA], [http://pdbe.org/5fw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5fw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fw5 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fw5 OCA], [https://pdbe.org/5fw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fw5 RCSB], [https://www.ebi.ac.uk/pdbsum/5fw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fw5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/G3BP1_HUMAN G3BP1_HUMAN]] May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.<ref>PMID:9889278</ref> <ref>PMID:11604510</ref> [[http://www.uniprot.org/uniprot/POLN_SFV POLN_SFV]] P123 is short-lived polyproteins, accumulating during early stage of infection. It localizes the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, it starts viral genome replication into antigenome. After these early events, P123 is cleaved sequentially into nsP1, nsP2 and nsP3. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex.<ref>PMID:8057461</ref> <ref>PMID:7831320</ref> <ref>PMID:8985362</ref> <ref>PMID:9811773</ref> <ref>PMID:10217401</ref> <ref>PMID:10748213</ref> <ref>PMID:16352561</ref> <ref>PMID:22514352</ref>  nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell.<ref>PMID:8057461</ref> <ref>PMID:7831320</ref> <ref>PMID:8985362</ref> <ref>PMID:9811773</ref> <ref>PMID:10217401</ref> <ref>PMID:10748213</ref> <ref>PMID:16352561</ref> <ref>PMID:22514352</ref>  nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Also inhibits cellular transcription by inducing rapid degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response.<ref>PMID:8057461</ref> <ref>PMID:7831320</ref> <ref>PMID:8985362</ref> <ref>PMID:9811773</ref> <ref>PMID:10217401</ref> <ref>PMID:10748213</ref> <ref>PMID:16352561</ref> <ref>PMID:22514352</ref>  nsP3 is essential for minus strand and subgenomic 26S mRNA synthesis.<ref>PMID:8057461</ref> <ref>PMID:7831320</ref> <ref>PMID:8985362</ref> <ref>PMID:9811773</ref> <ref>PMID:10217401</ref> <ref>PMID:10748213</ref> <ref>PMID:16352561</ref> <ref>PMID:22514352</ref>  nsP4 is an RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA codes for structural proteins.<ref>PMID:8057461</ref> <ref>PMID:7831320</ref> <ref>PMID:8985362</ref> <ref>PMID:9811773</ref> <ref>PMID:10217401</ref> <ref>PMID:10748213</ref> <ref>PMID:16352561</ref> <ref>PMID:22514352</ref> 
[https://www.uniprot.org/uniprot/G3BP1_HUMAN G3BP1_HUMAN] May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.<ref>PMID:9889278</ref> <ref>PMID:11604510</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Achour, A]]
[[Category: Homo sapiens]]
[[Category: Goette, B]]
[[Category: Large Structures]]
[[Category: Liu, L]]
[[Category: Semliki Forest virus]]
[[Category: McInerney, G M]]
[[Category: Achour A]]
[[Category: Panas, M D]]
[[Category: Goette B]]
[[Category: Schulte, T]]
[[Category: Liu L]]
[[Category: Thaa, B]]
[[Category: McInerney GM]]
[[Category: Hydrolase]]
[[Category: Panas MD]]
[[Category: Ras-gtpase activating protein sh3 domain binding protein g3bp1]]
[[Category: Schulte T]]
[[Category: Rasputin]]
[[Category: Thaa B]]
[[Category: Stress granule associated]]
[[Category: Transferase]]

Latest revision as of 13:29, 26 July 2023

Crystal structure of human G3BP1 in complex with Semliki Forest Virus nsP3-25 comprising two FGDF motives

5fw5, resolution 1.92Å

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