1ltl
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ltl' size='340' side='right'caption='[[1ltl]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1ltl' size='340' side='right'caption='[[1ltl]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ltl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ltl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1ltl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltl OCA], [https://pdbe.org/1ltl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltl RCSB], [https://www.ebi.ac.uk/pdbsum/1ltl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltl ProSAT]</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=1ltl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltl OCA], [https://pdbe.org/1ltl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltl RCSB], [https://www.ebi.ac.uk/pdbsum/1ltl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O27798_METTH O27798_METTH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1ltl ConSurf]. | </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=1ltl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Eukaryotic chromosomal DNA is licensed for replication precisely once in each cell cycle. The mini-chromosome maintenance (MCM) complex plays a role in this replication licensing. We have determined the structure of a fragment of MCM from Methanobacterium thermoautotrophicum (mtMCM), a model system for eukaryotic MCM. The structure reveals a novel dodecameric architecture with a remarkably long central channel. The channel surface has an unusually high positive charge and binds DNA. We also show that the structure of the N-terminal fragment is conserved for all MCMs proteins despite highly divergent sequences, suggesting a common architecture for a similar task: gripping/remodeling DNA and regulating MCM activity. An mtMCM mutant protein equivalent to a yeast MCM5 (CDC46) protein with the bob1 mutation at its N terminus has only subtle structural changes, suggesting a Cdc7-bypass mechanism by Bob1 in yeast. Yeast bypass experiments using MCM5 mutant proteins support the hypothesis for the bypass mechanism. | ||
| - | |||
| - | The structure and function of MCM from archaeal M. Thermoautotrophicum.,Fletcher RJ, Bishop BE, Leon RP, Sclafani RA, Ogata CM, Chen XS Nat Struct Biol. 2003 Mar;10(3):160-7. PMID:12548282<ref>PMID:12548282</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ltl" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Methanothermobacter thermautotrophicus]] |
| - | [[Category: | + | [[Category: Bishop BE]] |
| - | [[Category: | + | [[Category: Chen XS]] |
| - | [[Category: | + | [[Category: Fletcher RJ]] |
| - | [[Category: | + | [[Category: Leon RP]] |
| - | [[Category: | + | [[Category: Ogata CM]] |
| - | [[Category: | + | [[Category: Sclafani RA]] |
Current revision
THE DODECAMER STRUCTURE OF MCM FROM ARCHAEAL M. THERMOAUTOTROPHICUM
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