1bkn: Difference between revisions

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-[[Image:1bkn.gif|left|200px]]<br /><applet load="1bkn" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1bkn, resolution 2.9&Aring;" />
-'''CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL==
-MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in the MutL family that cause deficiencies in DNA mismatch repair and a predisposition to cancer mainly occur in the putative ATP-binding site. We provide evidence that the flexible, yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of the repair machinery.
+<StructureSection load='1bkn' size='340' side='right'caption='[[1bkn]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1bkn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BKN 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkn OCA], [https://pdbe.org/1bkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bkn RCSB], [https://www.ebi.ac.uk/pdbsum/1bkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bkn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MUTL_ECOLI MUTL_ECOLI] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA.
+== 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/bk/1bkn_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=1bkn ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-BKN is a [http://en.wikipedia.org/wiki/Single_protein 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=1BKN OCA].
+*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis., Ban C, Yang W, Cell. 1998 Nov 13;95(4):541-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9827806 9827806]
+[[Category: Escherichia coli K-12]]
-[[Category: Escherichia coli]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Ban C]]
-[[Category: Ban, C.]]
+[[Category: Yang W]]
-[[Category: Yang, W.]]
-[[Category: atpase]]
-[[Category: dna binding]]
-[[Category: dna repair]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:17 2008''