1b63

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{{Seed}}
 
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[[Image:1b63.png|left|200px]]
 
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==MUTL COMPLEXED WITH ADPNP==
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The line below this paragraph, containing "STRUCTURE_1b63", creates the "Structure Box" on the page.
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<StructureSection load='1b63' size='340' side='right'caption='[[1b63]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1b63]] is a 1 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=1B63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B63 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1b63| PDB=1b63 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b63 OCA], [https://pdbe.org/1b63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b63 RCSB], [https://www.ebi.ac.uk/pdbsum/1b63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b63 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/1b63_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1b63 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The MutL DNA mismatch repair protein has recently been shown to be an ATPase and to belong to an emerging ATPase superfamily that includes DNA topoisomerase II and Hsp90. We report here the crystal structures of a 40 kDa ATPase fragment of E. coli MutL (LN40) complexed with a substrate analog, ADPnP, and with product ADP. More than 60 residues that are disordered in the apoprotein structure become ordered and contribute to both ADPnP binding and dimerization of LN40. Hydrolysis of ATP, signified by subsequent release of the gamma-phosphate, releases two key loops and leads to dissociation of the LN40 dimer. Dimerization of the LN40 region is required for and is the rate-limiting step in ATP hydrolysis by MutL. The ATPase activity of MutL is stimulated by DNA and likely acts as a switch to coordinate DNA mismatch repair.
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===MUTL COMPLEXED WITH ADPNP===
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Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair.,Ban C, Junop M, Yang W Cell. 1999 Apr 2;97(1):85-97. PMID:10199405<ref>PMID:10199405</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1b63" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10199405}}, adds the Publication Abstract to the page
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*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10199405 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10199405}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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1B63 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=1B63 OCA].
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[[Category: Large Structures]]
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[[Category: Yang W]]
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==Reference==
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Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair., Ban C, Junop M, Yang W, Cell. 1999 Apr 2;97(1):85-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10199405 10199405]
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Yang, W.]]
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[[Category: Atpase]]
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[[Category: Dna mismatch repair]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:21:05 2008''
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Current revision

MUTL COMPLEXED WITH ADPNP

PDB ID 1b63

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