1rpr

From Proteopedia

(Difference between revisions)

Revision as of 07:19, 22 September 2021

THE STRUCTURE OF COLE1 ROP IN SOLUTION

Structural highlights

1rpr is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 structure of the ColE1 repressor of primer (rop) protein in solution was determined from the proton nuclear magnetic resonance data by a combined use of distance geometry and restrained molecular dynamics calculations. A set of structures was determined with low internal energy and virtually no violations of the experimental distance restraints. Rop forms homodimers: Two helical hairpins are arranged as an antiparallel four helix bundle with a left-handed rope-like twist of the helix axes and with left-handed bundle topology. The very compact packing of the side chains in the helix interfaces of the rop coiled-coil structure may well account for its high stability. Overall, the solution structure is highly similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces appear to influence the crystal structure.

The structure of ColE1 rop in solution.,Eberle W, Pastore A, Sander C, Rosch P J Biomol NMR. 1991 May;1(1):71-82. PMID:1841691^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Eberle W, Pastore A, Sander C, Rosch P. The structure of ColE1 rop in solution. J Biomol NMR. 1991 May;1(1):71-82. PMID:1841691

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rpr"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rpr' size='340' side='right'caption='[[1rpr]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RPR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RPR FirstGlance]. <br>
-</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=1rpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpr OCA], [http://pdbe.org/1rpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rpr RCSB], [http://www.ebi.ac.uk/pdbsum/1rpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rpr ProSAT]</span></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=1rpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpr OCA], [https://pdbe.org/1rpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rpr RCSB], [https://www.ebi.ac.uk/pdbsum/1rpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rpr ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1rpr

From Proteopedia

Revision as of 07:19, 22 September 2021

THE STRUCTURE OF COLE1 ROP IN SOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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