This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ul1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1ul1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ul1, resolution 2.9&Aring;" /> '''Crystal structure of...)
Current revision (23:55, 27 December 2023) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ul1.gif|left|200px]]<br />
 
-
<applet load="1ul1" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ul1, resolution 2.9&Aring;" />
 
-
'''Crystal structure of the human FEN1-PCNA complex'''<br />
 
-
==Overview==
+
==Crystal structure of the human FEN1-PCNA complex==
-
Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic, stability and replication. Proliferating cell nuclear antigen (PCNA) binds, FEN1 and stimulates its endonuclease activity. The structural basis of the, FEN1-PCNA interaction was revealed by the crystal structure of the complex, between human FEN1 and PCNA. The main interface involves the C-terminal, tail of FEN1, which forms two beta-strands connected by a short helix, the, betaA-alphaA-betaB motif, participating in beta-beta and hydrophobic, interactions with PCNA. These interactions are similar to those previously, observed for the p21CIP1/WAF1 peptide. However, this structure involving, the full-length enzyme has revealed additional interfaces that are, involved in the core domain. The interactions at the interfaces maintain, the enzyme in an inactive 'locked-down' orientation and might be utilized, in rapid DNA-tracking by preserving the central hole of PCNA for sliding, along the DNA. A hinge region present between the core domain and the, C-terminal tail of FEN1 would play a role in switching the FEN1, orientation from an inactive to an active orientation.
+
<StructureSection load='1ul1' size='340' side='right'caption='[[1ul1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ul1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The June 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Sliding Clamps'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_6 10.2210/rcsb_pdb/mom_2012_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UL1 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1ul1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul1 OCA], [https://pdbe.org/1ul1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ul1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ul1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ul1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FEN1_HUMAN FEN1_HUMAN] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.<ref>PMID:7961795</ref> <ref>PMID:8621570</ref> <ref>PMID:10744741</ref> <ref>PMID:11986308</ref> <ref>PMID:18443037</ref> <ref>PMID:20729856</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ul1_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ul1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic stability and replication. Proliferating cell nuclear antigen (PCNA) binds FEN1 and stimulates its endonuclease activity. The structural basis of the FEN1-PCNA interaction was revealed by the crystal structure of the complex between human FEN1 and PCNA. The main interface involves the C-terminal tail of FEN1, which forms two beta-strands connected by a short helix, the betaA-alphaA-betaB motif, participating in beta-beta and hydrophobic interactions with PCNA. These interactions are similar to those previously observed for the p21CIP1/WAF1 peptide. However, this structure involving the full-length enzyme has revealed additional interfaces that are involved in the core domain. The interactions at the interfaces maintain the enzyme in an inactive 'locked-down' orientation and might be utilized in rapid DNA-tracking by preserving the central hole of PCNA for sliding along the DNA. A hinge region present between the core domain and the C-terminal tail of FEN1 would play a role in switching the FEN1 orientation from an inactive to an active orientation.
-
==About this Structure==
+
Structural basis for recruitment of human flap endonuclease 1 to PCNA.,Sakurai S, Kitano K, Yamaguchi H, Hamada K, Okada K, Fukuda K, Uchida M, Ohtsuka E, Morioka H, Hakoshima T EMBO J. 2005 Feb 23;24(4):683-93. Epub 2004 Dec 16. PMID:15616578<ref>PMID:15616578</ref>
-
1UL1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UL1 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structural basis for recruitment of human flap endonuclease 1 to PCNA., Sakurai S, Kitano K, Yamaguchi H, Hamada K, Okada K, Fukuda K, Uchida M, Ohtsuka E, Morioka H, Hakoshima T, EMBO J. 2005 Feb 23;24(4):683-93. Epub 2004 Dec 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15616578 15616578]
+
</div>
-
[[Category: Homo sapiens]]
+
<div class="pdbe-citations 1ul1" style="background-color:#fffaf0;"></div>
-
[[Category: Protein complex]]
+
-
[[Category: Fukuda, K.]]
+
-
[[Category: Hakoshima, T.]]
+
-
[[Category: Hamada, K.]]
+
-
[[Category: Kitano, K.]]
+
-
[[Category: Morioka, H.]]
+
-
[[Category: Ohtsuka, E.]]
+
-
[[Category: Okada, K.]]
+
-
[[Category: Sakurai, S.]]
+
-
[[Category: Uchida, M.]]
+
-
[[Category: Yamaguchi, H.]]
+
-
[[Category: MG]]
+
-
[[Category: dna clamp]]
+
-
[[Category: dna repair]]
+
-
[[Category: dna-binding protein]]
+
-
[[Category: flap dna]]
+
-
[[Category: flap endonuclease]]
+
-
[[Category: hydrolase/dna binding protein complex]]
+
-
[[Category: protein complex]]
+
-
[[Category: replication]]
+
-
[[Category: sliding clamp]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:36:07 2007''
+
==See Also==
 +
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
 +
*[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: RCSB PDB Molecule of the Month]]
 +
[[Category: Sliding Clamps]]
 +
[[Category: Fukuda K]]
 +
[[Category: Hakoshima T]]
 +
[[Category: Hamada K]]
 +
[[Category: Kitano K]]
 +
[[Category: Morioka H]]
 +
[[Category: Ohtsuka E]]
 +
[[Category: Okada K]]
 +
[[Category: Sakurai S]]
 +
[[Category: Uchida M]]
 +
[[Category: Yamaguchi H]]

Current revision

Crystal structure of the human FEN1-PCNA complex

PDB ID 1ul1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ul1"
Personal tools