5fhh - Revision history

OCA at 06:51, 19 July 2023

2023-07-19T06:51:21Z

←Older revision		Revision as of 06:51, 19 July 2023
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	<StructureSection load='5fhh' size='340' side='right'caption='[[5fhh]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='5fhh' size='340' side='right'caption='[[5fhh]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fhh]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5FHH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fhh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FHH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ADP:ADENOSINE~~-~~5-DIPHOSPHATE'>ADP</scene>~~, ~~<scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</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]] 3.6Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:]]</b></td><td class="sblockDat">[[5fhd\|5fhd]], [[5fhe\|5fhe]], [[5fhf\|5fhf]], [[5fhg\|5fhg~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PIF1, C15orf20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</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=5fhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhh OCA], [https://pdbe.org/5fhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fhh RCSB], [https://www.ebi.ac.uk/pdbsum/5fhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhh ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12]~~ </~~span~~></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=5fhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhh OCA], [~~http~~://pdbe.org/5fhh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fhh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fhh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhh ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PIF1_HUMAN PIF1_HUMAN]] DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity.[HAMAP-Rule:MF_03176]<ref>PMID:16522649</ref> <ref>PMID:17172855</ref> <ref>PMID:17827721</ref> <ref>PMID:18835853</ref> <ref>PMID:19700773</ref> <ref>PMID:20524933</ref> <ref>PMID:23657261</ref>	+	[https://www.uniprot.org/uniprot/PIF1_HUMAN PIF1_HUMAN] DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity.[HAMAP-Rule:MF_03176]<ref>PMID:16522649</ref> <ref>PMID:17172855</ref> <ref>PMID:17827721</ref> <ref>PMID:18835853</ref> <ref>PMID:19700773</ref> <ref>PMID:20524933</ref> <ref>PMID:23657261</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: ~~DNA helicase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[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: Hydrolase]]~~	+
-	~~[[Category: Pif1 helicase]]~~	+
-	~~[[Category: Sf1b 5'-3' dna helicase~~]]	+

OCA at 07:20, 6 May 2020

2020-05-06T07:20:02Z

←Older revision		Revision as of 07:20, 6 May 2020
Line 1:		Line 1:

	==Structure of human Pif1 helicase domain residues 200-641==		==Structure of human Pif1 helicase domain residues 200-641==
-	<StructureSection load='5fhh' size='340' side='right' caption='[[5fhh]], [[Resolution\|resolution]] 3.60Å' scene=''>	+	<StructureSection load='5fhh' size='340' side='right'caption='[[5fhh]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fhh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHH OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FHH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fhh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FHH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5fhd\|5fhd]], [[5fhe\|5fhe]], [[5fhf\|5fhf]], [[5fhg\|5fhg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5fhd\|5fhd]], [[5fhe\|5fhe]], [[5fhf\|5fhf]], [[5fhg\|5fhg]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIF1, C15orf20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=5fhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhh OCA], [http://pdbe.org/5fhh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fhh RCSB], [http://www.ebi.ac.uk/pdbsum/5fhh PDBsum]</span></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=5fhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhh OCA], [http://pdbe.org/5fhh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fhh RCSB], [http://www.ebi.ac.uk/pdbsum/5fhh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5fhh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fhh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Helicase 3D structures\|Helicase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bharath, S R]]		[[Category: Bharath, S R]]
	[[Category: Ren, W]]		[[Category: Ren, W]]

OCA at 20:34, 11 May 2016

2016-05-11T20:34:18Z

←Older revision		Revision as of 20:34, 11 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5fhh is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of human Pif1 helicase domain residues 200-641==
		+	<StructureSection load='5fhh' size='340' side='right' caption='[[5fhh]], [[Resolution\|resolution]] 3.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5fhh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FHH FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5fhd\|5fhd]], [[5fhe\|5fhe]], [[5fhf\|5fhf]], [[5fhg\|5fhg]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=5fhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhh OCA], [http://pdbe.org/5fhh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fhh RCSB], [http://www.ebi.ac.uk/pdbsum/5fhh PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PIF1_HUMAN PIF1_HUMAN]] DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity.[HAMAP-Rule:MF_03176]<ref>PMID:16522649</ref> <ref>PMID:17172855</ref> <ref>PMID:17827721</ref> <ref>PMID:18835853</ref> <ref>PMID:19700773</ref> <ref>PMID:20524933</ref> <ref>PMID:23657261</ref>
		+	<div style="background-color:#fffaf0;">
		+	== 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.

-	~~Authors: Zhou~~, X., Ren, W., Bharath, ~~S.R.~~, ~~Song~~, H.	+	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<ref>PMID:26904952</ref>

-	~~Description: Structure~~ of ~~human Pif1 helicase domain residues 200~~-~~641~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	[[Category: ~~Zhou, X~~]]	+	<div class="pdbe-citations 5fhh" style="background-color:#fffaf0;"></div>
-	[[Category: Bharath, S.R]]	+	== References ==
-	~~[[Category: Song, H~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: DNA helicase]]
		+	[[Category: Bharath, S R]]
	[[Category: Ren, W]]		[[Category: Ren, W]]
		+	[[Category: Song, H]]
		+	[[Category: Zhou, X]]
		+	[[Category: Hydrolase]]
		+	[[Category: Pif1 helicase]]
		+	[[Category: Sf1b 5'-3' dna helicase]]

OCA at 13:03, 3 February 2016

2016-02-03T13:03:08Z

←Older revision		Revision as of 13:03, 3 February 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5fhh is ON HOLD	+	The entry 5fhh is ON HOLD until Paper Publication

	Authors: Zhou, X., Ren, W., Bharath, S.R., Song, H.		Authors: Zhou, X., Ren, W., Bharath, S.R., Song, H.

OCA: Protected "5fhh" [edit=sysop:move=sysop]

2015-12-30T17:57:55Z

Protected "5fhh" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:57, 30 December 2015

OCA: New page: '''Unreleased structure''' The entry 5fhh is ON HOLD Authors: Zhou, X., Ren, W., Bharath, S.R., Song, H. Description: Structure of human Pif1 helicase domain residues 200-641 [[Categor...

2015-12-30T17:57:54Z

New page: '''Unreleased structure''' The entry 5fhh is ON HOLD Authors: Zhou, X., Ren, W., Bharath, S.R., Song, H. Description: Structure of human Pif1 helicase domain residues 200-641 [[Categor...

New page

'''Unreleased structure'''

The entry 5fhh is ON HOLD

Authors: Zhou, X., Ren, W., Bharath, S.R., Song, H.

Description: Structure of human Pif1 helicase domain residues 200-641
[[Category: Unreleased Structures]]
[[Category: Zhou, X]]
[[Category: Bharath, S.R]]
[[Category: Song, H]]
[[Category: Ren, W]]