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5fhg

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Revision as of 06:51, 19 July 2023

Structure of unliganded Pif1 from Bacteroides sp

Structural highlights

5fhg is a 2 chain structure with sequence from Bacteroides fragilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Pif1 is a conserved SF1B DNA helicase involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. Here, we report the structures of the helicase domain of human Pif1 and Bacteroides sp Pif1 (BaPif1) in complex with ADP-AlF4(-) and two different single-stranded DNAs (ssDNAs). The wedge region equivalent to the beta hairpin in other SF1B DNA helicases folds into an extended loop followed by an alpha helix. The Pif1 signature motif of BaPif1 interacts with the wedge region and a short helix in order to stabilize these ssDNA binding elements, therefore indirectly exerting its functional role. Domain 2B of BaPif1 undergoes a large conformational change upon concomitant binding of ATP and ssDNA, which is critical for Pif1's activities. BaPif1 cocrystallized with a tailed dsDNA and ADP-AlF4(-), resulting in a bound ssDNA bent nearly 90 degrees at the ssDNA/dsDNA junction. The conformational snapshots of BaPif1 provide insights into the mechanism governing the helicase activity of Pif1.

Structural and Functional Insights into the Unwinding Mechanism of Bacteroides sp Pif1.,Zhou X, Ren W, Bharath SR, Tang X, He Y, Chen C, Liu Z, Li D, Song H Cell Rep. 2016 Mar 1;14(8):2030-9. doi: 10.1016/j.celrep.2016.02.008. Epub 2016, Feb 18. PMID:26904952^[1]

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

References

↑ Zhou X, Ren W, Bharath SR, Tang X, He Y, Chen C, Liu Z, Li D, Song H. Structural and Functional Insights into the Unwinding Mechanism of Bacteroides sp Pif1. Cell Rep. 2016 Mar 1;14(8):2030-9. doi: 10.1016/j.celrep.2016.02.008. Epub 2016, Feb 18. PMID:26904952 doi:http://dx.doi.org/10.1016/j.celrep.2016.02.008

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5fhg"

@@ Line 3: / Line 3: @@
 <StructureSection load='5fhg' size='340' side='right'caption='[[5fhg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5fhg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FHG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5fhg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FHG FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fhd|5fhd]], [[5fhe|5fhe]], [[5fhf|5fhf]], [[5fhh|5fhh]]</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&#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=5fhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhg OCA], [http://pdbe.org/5fhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fhg RCSB], [http://www.ebi.ac.uk/pdbsum/5fhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhg 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=5fhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhg OCA], [https://pdbe.org/5fhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fhg RCSB], [https://www.ebi.ac.uk/pdbsum/5fhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhg ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 20: / Line 20: @@
 __TOC__
 </StructureSection>
+[[Category: Bacteroides fragilis]]
 [[Category: Large Structures]]
-[[Category: Bharath, S R]]
+[[Category: Bharath SR]]
-[[Category: Ren, W]]
+[[Category: Ren W]]
-[[Category: Song, H]]
+[[Category: Song H]]
-[[Category: Zhou, X]]
+[[Category: Zhou X]]
-[[Category: Dna helicase]]
-[[Category: Hydrolase]]
-[[Category: Pif1 helicase]]

5fhg

From Proteopedia

Revision as of 06:51, 19 July 2023

Structure of unliganded Pif1 from Bacteroides sp

Structural highlights

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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