1nlf: Difference between revisions

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-[[Image:1nlf.jpg|left|200px]]
- {{Structure
+==Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution==
-|PDB= 1nlf |SIZE=350|CAPTION= <scene name='initialview01'>1nlf</scene>, resolution 1.95&Aring;
+<StructureSection load='1nlf' size='340' side='right'caption='[[1nlf]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1nlf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NLF FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-|GENE= REPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlf OCA], [https://pdbe.org/1nlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nlf RCSB], [https://www.ebi.ac.uk/pdbsum/1nlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nlf ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlf OCA], [http://www.ebi.ac.uk/pdbsum/1nlf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nlf RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/REPJ_ECOLX REPJ_ECOLX] This protein is involved in regulating the plasmid copy-number. Increasing the level of this protein results in a higher plasmid copy-number.
+== 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/nl/1nlf_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=1nlf ConSurf].
+<div style="clear:both"></div>
-'''Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution'''
+==See Also==
+*[[Helicase 3D structures|Helicase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The structure of a new crystal form (space group C2), grown at pH 8.0 and diffracting to 1.95 A resolution, of the replicative homo-hexameric DNA helicase RepA encoded by plasmid RSF1010 is reported. In contrast to previous crystals grown at pH 6.0 in space group P2(1) (Niedenzu et al., 2001), only one half (a trimer) of the RepA hexamer occupies the asymmetric unit of the space-group C2 crystals. The new crystal packing explains the pH-dependent hexamer-hexamer association mechanism of RepA. The C-terminus (264)VLERQRKSKGVPRGEA(279), which could not be modelled in the previous structure, is clearly defined in the present electron density except for the last four amino acids. Sulfate anions occupy the six ATPase active sites of RepA at positions where the product phosphates are supposed to bind. Binding of sulfate anions induces conformational changes both at the ATPase active sites and throughout the whole molecular structure. In agreement with electron microscopy, the above studies implicate structural changes to an "open" form that may occur upon binding and hydrolysis of nucleotide 5'-triphosphates and could be essential for DNA duplex-unwinding activity.
-==About this Structure==
-NLF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLF OCA].
-==Reference==
-Structure of DNA helicase RepA in complex with sulfate at 1.95 A resolution implicates structural changes to an "open" form., Xu H, Strater N, Schroder W, Bottcher C, Ludwig K, Saenger W, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):815-22. Epub 2003, Apr 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12777796 12777796]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bottcher, C.]]
+[[Category: Bottcher C]]
-[[Category: Ludwig, K.]]
+[[Category: Ludwig K]]
-[[Category: Saenger, W.]]
+[[Category: Saenger W]]
-[[Category: Schroeder, W.]]
+[[Category: Schroeder W]]
-[[Category: Strater, N.]]
+[[Category: Strater N]]
-[[Category: Xu, H.]]
+[[Category: Xu H]]
-[[Category: replicative dna helicase structural change]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:32:00 2008''