4c30: Difference between revisions

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 <StructureSection load='4c30' size='340' side='right'caption='[[4c30]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c30]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C30 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c30]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] 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=4C30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C30 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c2t|4c2t]], [[4c2u|4c2u]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4c30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c30 OCA], [https://pdbe.org/4c30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c30 RCSB], [https://www.ebi.ac.uk/pdbsum/4c30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c30 ProSAT]</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=4c30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c30 OCA], [http://pdbe.org/4c30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c30 RCSB], [http://www.ebi.ac.uk/pdbsum/4c30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c30 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q9RTI9_DEIRA Q9RTI9_DEIRA]
-DNA helicases are responsible for unwinding the duplex DNA, a key step in many biological processes. UvrD is a DNA helicase involved in several DNA repair pathways. We report here crystal structures of Deinococcus radiodurans UvrD (drUvrD) in complex with DNA in different nucleotide-free and bound states. These structures provide us with three distinct snapshots of drUvrD in action and for the first time trap a DNA helicase undergoing a large-scale spiral movement around duplexed DNA. Our structural data also improve our understanding of the molecular mechanisms that regulate DNA unwinding by Superfamily 1A (SF1A) helicases. Our biochemical data reveal that drUvrD is a DNA-stimulated ATPase, can translocate along ssDNA in the 3'-5' direction and shows ATP-dependent 3'-5', and surprisingly also, 5'-3' helicase activity. Interestingly, we find that these translocase and helicase activities of drUvrD are modulated by the ssDNA binding protein. Analysis of drUvrD mutants indicate that the conserved beta-hairpin structure of drUvrD that functions as a separation pin is critical for both drUvrD's 3'-5' and 5'-3' helicase activities, whereas the GIG motif of drUvrD involved in binding to the DNA duplex is essential for the 5'-3' helicase activity only. These special features of drUvrD may reflect its involvement in a wide range of DNA repair processes in vivo.
-Structural and Mechanistic Insight into DNA Unwinding by Deinococcus radiodurans UvrD.,Stelter M, Acajjaoui S, McSweeney S, Timmins J PLoS One. 2013 Oct 15;8(10):e77364. doi: 10.1371/journal.pone.0077364. PMID:24143224<ref>PMID:24143224</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4c30" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Helicase|Helicase]]
+*[[Helicase 3D structures|Helicase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Micrococcus radiodurans raj et al. 1960]]
+[[Category: Deinococcus radiodurans]]
-[[Category: DNA helicase]]
 [[Category: Large Structures]]
-[[Category: Acajjaoui, S]]
+[[Category: Synthetic construct]]
-[[Category: McSweeney, S]]
+[[Category: Acajjaoui S]]
-[[Category: Stelter, M]]
+[[Category: McSweeney S]]
-[[Category: Timmins, J]]
+[[Category: Stelter M]]
-[[Category: Dna helicase]]
+[[Category: Timmins J]]
-[[Category: Dna repair]]
-[[Category: Hydrolase-dna complex]]
-[[Category: Nucleotide excision repair]]