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| | ==Novel Crystal Form of the ColE1 Rom Protein== | | ==Novel Crystal Form of the ColE1 Rom Protein== |
| - | <StructureSection load='2ghy' size='340' side='right' caption='[[2ghy]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='2ghy' size='340' side='right'caption='[[2ghy]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ghy]] 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=2GHY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GHY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ghy]] 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=2GHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GHY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rop|1rop]]</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]] 2.5Å</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=2ghy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghy OCA], [https://pdbe.org/2ghy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ghy RCSB], [https://www.ebi.ac.uk/pdbsum/2ghy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ghy 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=2ghy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghy OCA], [http://pdbe.org/2ghy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ghy RCSB], [http://www.ebi.ac.uk/pdbsum/2ghy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ghy 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/Q7BLB4_ECOLX Q7BLB4_ECOLX] [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: Carter, R J]] | + | [[Category: Large Structures]] |
| - | [[Category: Comolli, L R]] | + | [[Category: Carter RJ]] |
| - | [[Category: Holbrook, E L]] | + | [[Category: Comolli LR]] |
| - | [[Category: Holbrook, S R]] | + | [[Category: Holbrook EL]] |
| - | [[Category: Jang, S B]] | + | [[Category: Holbrook SR]] |
| - | [[Category: Jeong, M S]] | + | [[Category: Jang SB]] |
| - | [[Category: Hiv-1]] | + | [[Category: Jeong MS]] |
| - | [[Category: Kissing hairpin]]
| + | |
| - | [[Category: Rna one modulator protein]]
| + | |
| - | [[Category: Structural packing]]
| + | |
| - | [[Category: Transcription]]
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| Structural highlights
Function
Q7BLB4_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
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 RNA I modulator protein (Rom) acts as a co-regulator of ColE1 plasmid copy number by binding to RNA kissing hairpins and stabilizing their interaction. The structure of Rom has been determined in a new crystal form from X-ray diffraction data to 2.5 A resolution. In this structure, a dimer of the 57-amino-acid protein is found in the asymmetric unit. Each subunit consists almost entirely of two antiparallel alpha-helices joined by a short hairpin bend. The dimer contains a non-crystallographic twofold axis and forms a highly regular four-alpha-helical bundle. The structural packing in this novel crystal form is different from previously known Rom structures. The asymmetric unit contains one dimer, giving a crystal volume per protein weight (V(M)) of 1.83 A(3) Da(-1) and a low solvent content of 30%. Strong packing interactions and low solvation are characteristic of the structure. The Rom protein was cocrystallized with the Tar-Tar* kissing hairpin RNA. Although the electron-density maps do not show bound RNA, altered conformations in the side chains of Rom that are known to be involved in RNA binding have been identified. These results provide additional information about Rom protein conformational flexibility and suggest that the presence of a highly charged polymer such as RNA can promote tight packing of an RNA-binding protein, even when the RNA itself is not observed in the crystal.
Novel crystal form of the ColE1 Rom protein.,Jang SB, Jeong MS, Carter RJ, Holbrook EL, Comolli LR, Holbrook SR Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):619-27. Epub 2006, May 12. PMID:16699189[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jang SB, Jeong MS, Carter RJ, Holbrook EL, Comolli LR, Holbrook SR. Novel crystal form of the ColE1 Rom protein. Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):619-27. Epub 2006, May 12. PMID:16699189 doi:10.1107/S0907444906012388
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