|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution NMR structure of the cell division regulator MinE protein from Neisseria gonorrhoeae== | | ==Solution NMR structure of the cell division regulator MinE protein from Neisseria gonorrhoeae== |
| - | <StructureSection load='2kxo' size='340' side='right'caption='[[2kxo]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2kxo' size='340' side='right'caption='[[2kxo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kxo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus gonorrhoeae" (zopf 1885) lehmann and neumann 1896]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kxo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXO FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">minE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</td></tr> | + | </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=2kxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxo OCA], [https://pdbe.org/2kxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxo RCSB], [https://www.ebi.ac.uk/pdbsum/2kxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxo 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=2kxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxo OCA], [https://pdbe.org/2kxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxo RCSB], [https://www.ebi.ac.uk/pdbsum/2kxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MINE_NEIGO MINE_NEIGO]] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell (By similarity).
| + | [https://www.uniprot.org/uniprot/MINE_NEIGO MINE_NEIGO] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ducat, T]] | |
| - | [[Category: Ghasriani, H]] | |
| - | [[Category: Goto, N K]] | |
| - | [[Category: Cell cycle]] | |
| - | [[Category: Cell division]] | |
| - | [[Category: Mind-binding]] | |
| - | [[Category: Mine]] | |
| | [[Category: Neisseria gonorrhoeae]] | | [[Category: Neisseria gonorrhoeae]] |
| - | [[Category: Topological specificity]] | + | [[Category: Ducat T]] |
| | + | [[Category: Ghasriani H]] |
| | + | [[Category: Goto NK]] |
| Structural highlights
Function
MINE_NEIGO Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell (By similarity).
Publication Abstract from PubMed
MinE is required for the dynamic oscillation of Min proteins that restricts formation of the cytokinetic septum to the midpoint of the cell in gram negative bacteria. Critical for this oscillation is MinD-binding by MinE to stimulate MinD ATP hydrolysis, a function that had been assigned to the first approximately 30 residues in MinE. Previous models based on the structure of an autonomously folded dimeric C-terminal fragment suggested that the N-terminal domain is freely accessible for interactions with MinD. We report here the solution NMR structure of the full-length MinE dimer from Neisseria gonorrhoeae, with two parts of the N-terminal domain forming an integral part of the dimerization interface. Unexpectedly, solvent accessibility is highly restricted for residues that were previously hypothesized to directly interact with MinD. To delineate the true MinD-binding region, in vitro assays for MinE-stimulated MinD activity were performed. The relative MinD-binding affinities obtained for full-length and N-terminal peptides from MinE demonstrated that residues that are buried in the dimeric interface nonetheless participate in direct interactions with MinD. According to results from NMR spin relaxation experiments, access to these buried residues may be facilitated by the presence of conformational exchange. We suggest that this concealment of MinD-binding residues by the MinE dimeric interface provides a mechanism for prevention of nonspecific interactions, particularly with the lipid membrane, to allow the free diffusion of MinE that is critical for Min protein oscillation.
Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE.,Ghasriani H, Ducat T, Hart CT, Hafizi F, Chang N, Al-Baldawi A, Ayed SH, Lundstrom P, Dillon JA, Goto NK Proc Natl Acad Sci U S A. 2010 Oct 11. PMID:20937912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghasriani H, Ducat T, Hart CT, Hafizi F, Chang N, Al-Baldawi A, Ayed SH, Lundstrom P, Dillon JA, Goto NK. Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE. Proc Natl Acad Sci U S A. 2010 Oct 11. PMID:20937912 doi:10.1073/pnas.1007141107
|
