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| | <StructureSection load='3k79' size='340' side='right'caption='[[3k79]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='3k79' size='340' side='right'caption='[[3k79]], [[Resolution|resolution]] 1.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k79]] is a 1 chain structure with sequence from [https://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=3K79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K79 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k79]] is a 1 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=3K79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K79 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rop ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 1.96Å</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=3k79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k79 OCA], [https://pdbe.org/3k79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k79 RCSB], [https://www.ebi.ac.uk/pdbsum/3k79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k79 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=3k79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k79 OCA], [https://pdbe.org/3k79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k79 RCSB], [https://www.ebi.ac.uk/pdbsum/3k79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k79 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hari, S B]] | + | [[Category: Hari SB]] |
| - | [[Category: Magliery, T J]] | + | [[Category: Magliery TJ]] |
| - | [[Category: Cysteine-free]]
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| - | [[Category: Four-helix bundle]]
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| - | [[Category: Hairpin]]
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| - | [[Category: Plasmid]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulation]]
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| 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
Cysteine residues can complicate the folding and storage of proteins due to improper formation of disulfide bonds or oxidation of residues that are natively reduced. Wild-type Rop is a homodimeric four-helix bundle protein and an important model for protein design in the understanding of protein stability, structure and folding kinetics. In the native state, Rop has two buried, reduced cysteine residues in its core, but these are prone to oxidation in destabilized variants, particularly upon extended storage. To circumvent this problem, we designed and characterized a Cys-free variant of Rop, including solving the 2.3 A X-ray crystal structure. We show that the C38A C52V variant has similar structure, stability and in vivo activity to wild-type Rop, but that it has dramatically faster unfolding kinetics like virtually every other mutant of Rop that has been characterized. This cysteine-free Rop has already proven useful for studies on solution topology and on the relationship of core mutations to stability. It also suggests a general strategy for removal of pairs of Cys residues in proteins, both to make them more experimentally tractable and to improve their storage properties for therapeutic or industrial purposes.
Cysteine-free Rop: A four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics.,Hari SB, Byeon C, Lavinder JJ, Magliery TJ Protein Sci. 2010 Jan 21. PMID:20095056[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hari SB, Byeon C, Lavinder JJ, Magliery TJ. Cysteine-free Rop: A four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics. Protein Sci. 2010 Jan 21. PMID:20095056 doi:10.1002/pro.342
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