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6lmj

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ASFV pA104R in complex with double-strand DNA

Structural highlights

6lmj is a 4 chain structure with sequence from African swine fever virus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VHLP_ASFB7 DNA-binding protein that plays a critical role in nucleoid compaction, genome replication and DNA replication and transcription (PubMed:28381576). Binds to both ssDNA and dsDNA with a binding site covering about 15 nucleotides (PubMed:28381576). Displays DNA-supercoiling activity only when associated with the viral DNA topoisomerase 2 (PubMed:28381576).^[1]

Publication Abstract from PubMed

African swine fever virus (ASFV) is a highly contagious nucleocytoplasmic large DNA virus (NCLDV) that causes nearly 100% mortality in swine. The development of effective vaccines and drugs against this virus is urgently needed. pA104R, an ASFV-derived histone-like protein, shares sequence and functional similarity with bacterial HU/IHF family members and is essential for viral replication. Herein, we solved the crystal structures of pA104R in its apo state as well as in complex with DNA. Apo-pA104R forms a homodimer and folds into an architecture conserved in bacterial heat-unstable nucleoid proteins/integration host factors (HUs/IHFs). The pA104R-DNA complex structure, however, uncovers that pA104R has a DNA binding pattern distinct from its bacterial homologs, that is, the beta-ribbon arms of pA104R stabilize DNA binding by contacting the major groove instead of the minor groove. Mutations of the basic residues at the base region of the beta-strand DNA binding region (BDR), rather than those in the beta-ribbon arms, completely abolished DNA binding, highlighting the major role of the BDR base in DNA binding. An overall DNA bending angle of 93.8 degrees is observed in crystal packing of the pA104R-DNA complex structure, which is close to the DNA bending angle in the HU-DNA complex. Stilbene derivatives SD1 and SD4 were shown to disrupt the binding between pA104R and DNA and inhibit the replication of ASFV in primary porcine alveolar macrophages. Collectively, these results reveal the structural basis of pA104R binding to DNA highlighting the importance of the pA104R-DNA interaction in the ASFV replication cycle and provide inhibitor leads for ASFV chemotherapy.

The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives.,Liu R, Sun Y, Chai Y, Li S, Li S, Wang L, Su J, Yu S, Yan J, Gao F, Zhang G, Qiu HJ, Gao GF, Qi J, Wang H Proc Natl Acad Sci U S A. 2020 May 1. pii: 1922523117. doi:, 10.1073/pnas.1922523117. PMID:32358196^[2]

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

References

↑ Frouco G, Freitas FB, Coelho J, Leitão A, Martins C, Ferreira F. DNA-Binding Properties of African Swine Fever Virus pA104R, a Histone-Like Protein Involved in Viral Replication and Transcription. J Virol. 2017 May 26;91(12):e02498-16. PMID:28381576 doi:10.1128/JVI.02498-16
↑ Liu R, Sun Y, Chai Y, Li S, Li S, Wang L, Su J, Yu S, Yan J, Gao F, Zhang G, Qiu HJ, Gao GF, Qi J, Wang H. The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives. Proc Natl Acad Sci U S A. 2020 May 1. pii: 1922523117. doi:, 10.1073/pnas.1922523117. PMID:32358196 doi:http://dx.doi.org/10.1073/pnas.1922523117

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/6lmj"

@@ Line 3: / Line 3: @@
 <StructureSection load='6lmj' size='340' side='right'caption='[[6lmj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6lmj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Asf Asf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LMJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LMJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6lmj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LMJ FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A104R, A104R CDS, BA71V-A104R, AFSV47Ss_0056, ASFV-Georgia_4-058 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10497 ASF])</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]] 2.8&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lmj OCA], [http://pdbe.org/6lmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lmj RCSB], [http://www.ebi.ac.uk/pdbsum/6lmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lmj ProSAT]</span></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=6lmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lmj OCA], [https://pdbe.org/6lmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lmj RCSB], [https://www.ebi.ac.uk/pdbsum/6lmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lmj ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/VHLP_ASFB7 VHLP_ASFB7] DNA-binding protein that plays a critical role in nucleoid compaction, genome replication and DNA replication and transcription (PubMed:28381576). Binds to both ssDNA and dsDNA with a binding site covering about 15 nucleotides (PubMed:28381576). Displays DNA-supercoiling activity only when associated with the viral DNA topoisomerase 2 (PubMed:28381576).<ref>PMID:28381576</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Asf]]
+[[Category: African swine fever virus]]
 [[Category: Large Structures]]
-[[Category: Chai, Y]]
+[[Category: Synthetic construct]]
-[[Category: Gao, F]]
+[[Category: Chai Y]]
-[[Category: Liu, R]]
+[[Category: Gao F]]
-[[Category: Qi, J]]
+[[Category: Liu R]]
-[[Category: Wang, H]]
+[[Category: Qi J]]
-[[Category: Asfv]]
+[[Category: Wang H]]
-[[Category: Complex]]
-[[Category: Dna binding protein]]
-[[Category: Dna binding protein-dna complex]]
-[[Category: Dsdna]]

6lmj

From Proteopedia

Current revision

ASFV pA104R in complex with double-strand DNA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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