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| | ==Crystal structure of a five-residue deletion mutant of the Rop protein== | | ==Crystal structure of a five-residue deletion mutant of the Rop protein== |
| - | <StructureSection load='1qx8' size='340' side='right' caption='[[1qx8]], [[Resolution|resolution]] 2.02Å' scene=''> | + | <StructureSection load='1qx8' size='340' side='right'caption='[[1qx8]], [[Resolution|resolution]] 2.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qx8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qx8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QX8 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rop|1rop]], [[1rpo|1rpo]], [[1b6q|1b6q]], [[1gmg|1gmg]]</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]] 2.02Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rop ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1qx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx8 OCA], [https://pdbe.org/1qx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qx8 RCSB], [https://www.ebi.ac.uk/pdbsum/1qx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx8 ProSAT]</span></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=1qx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx8 OCA], [http://pdbe.org/1qx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1qx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX]] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events. | + | [https://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Cesareni, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Glykos, N M]] | + | [[Category: Cesareni G]] |
| - | [[Category: Kokkinidis, M]] | + | [[Category: Glykos NM]] |
| - | [[Category: Kotsifaki, D]] | + | [[Category: Kokkinidis M]] |
| - | [[Category: Papanikolaou, Y]] | + | [[Category: Kotsifaki D]] |
| - | [[Category: Vlassi, M]] | + | [[Category: Papanikolaou Y]] |
| - | [[Category: Initiation of transcription]]
| + | [[Category: Vlassi M]] |
| - | [[Category: Replication]]
| + | |
| - | [[Category: Rna primer]]
| + | |
| - | [[Category: Transcription]]
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| - | [[Category: X-ray]]
| + | |
| Structural highlights
Function
ROP_ECOLX Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The repressor of primer (Rop) protein has become a steady source of surprises concerning the relationship between the sequences and the structures of several of its mutants and variants. Here we add another piece to the puzzle of Rop by showing that an engineered deletion mutant of the protein (corresponding to a deletion of residues 30-34 of the wild-type protein and designed to restore the heptad periodicity at the turn region) results in a complete reorganization of the bundle which is converted from a homodimer to a homotetramer. In contrast (and as previously shown), a two-residue insertion, which also restores the heptad periodicity, is essentially identical with wild-type Rop. The new deletion mutant structure is a canonical, left-handed, all-antiparallel bundle with a completely different hydrophobic core and distinct surface properties. The structure agrees and qualitatively explains the results from functional, thermodynamic, and kinetic studies which indicated that this deletion mutant is a biologically inactive hyperstable homotetramer. Additional insight into the stability and dynamics of the mutant structure has been obtained from extensive molecular dynamics simulations in explicit water and with full treatment of electrostatics.
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein.,Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:16953576[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M. Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein. Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:16953576 doi:10.1021/bi060833n
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