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| ==NgoL== | | ==NgoL== |
| <StructureSection load='3ncv' size='340' side='right' caption='[[3ncv]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3ncv' size='340' side='right'caption='[[3ncv]], [[Resolution|resolution]] 2.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3ncv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neig1 Neig1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NCV FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3ncv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NCV FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mutL, NGO0744, NgoL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242231 NEIG1])</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]] 2.4Å</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=3ncv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncv OCA], [http://pdbe.org/3ncv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ncv RCSB], [http://www.ebi.ac.uk/pdbsum/3ncv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ncv 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=3ncv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncv OCA], [https://pdbe.org/3ncv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ncv RCSB], [https://www.ebi.ac.uk/pdbsum/3ncv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ncv ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/MUTL_NEIG1 MUTL_NEIG1] |
| The mismatch repair (MMR) pathway serves to maintain the integrity of the genome by removing mispaired bases from the newly synthesized strand. In E. coli, MutS, MutL and MutH coordinate to discriminate the daughter strand through a mechanism involving lack of methylation on the new strand. This facilitates the creation of a nick by MutH in the daughter strand to initiate mismatch repair. Many bacteria and eukaryotes, including humans, do not possess a homolog of MutH. Although the exact strategy for strand discrimination in these organisms is yet to be ascertained, the required nicking endonuclease activity is resident in the C-terminal domain of MutL. This activity is dependent on the integrity of a conserved metal binding motif. Unlike their eukaryotic counterparts, MutL in bacteria like Neisseria exist in the form of a homodimer. Even though this homodimer would possess two active sites, it still acts a nicking endonuclease. Here, we present the crystal structure of the C-terminal domain (CTD) of the MutL homolog of Neisseria gonorrhoeae (NgoL) determined to a resolution of 2.4 A. The structure shows that the metal binding motif exists in a helical configuration and that four of the six conserved motifs in the MutL family, including the metal binding site, localize together to form a composite active site. NgoL-CTD exists in the form of an elongated inverted homodimer stabilized by a hydrophobic interface rich in leucines. The inverted arrangement places the two composite active sites in each subunit on opposite lateral sides of the homodimer. Such an arrangement raises the possibility that one of the active sites is occluded due to interaction of NgoL with other protein factors involved in MMR. The presentation of only one active site to substrate DNA will ensure that nicking of only one strand occurs to prevent inadvertent and deleterious double stranded cleavage.
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| The C-terminal domain of the MutL homolog from Neisseria gonorrhoeae forms an inverted homodimer.,Namadurai S, Jain D, Kulkarni DS, Tabib CR, Friedhoff P, Rao DN, Nair DT PLoS One. 2010 Oct 28;5(10):e13726. PMID:21060849<ref>PMID:21060849</ref>
| | ==See Also== |
| | | *[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3ncv" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Neig1]] | | [[Category: Large Structures]] |
| [[Category: Jain, D]] | | [[Category: Neisseria gonorrhoeae FA 1090]] |
| [[Category: Nair, D T]] | | [[Category: Jain D]] |
| [[Category: Namadurai, S]] | | [[Category: Nair DT]] |
| [[Category: Dimer]] | | [[Category: Namadurai S]] |
| [[Category: Endonuclease]]
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| [[Category: Hydrolase]]
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| [[Category: Repair]]
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