4do2

From Proteopedia

(Difference between revisions)

Revision as of 09:33, 7 February 2015

Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.

Structural highlights

4do2 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1rop
Gene:	rop ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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.

Publication Abstract from PubMed

The dimeric Repressor of Primer (Rop) protein, a widely used model system for the study of coiled-coil 4-alpha-helical bundles, is characterized by a remarkable structural plasticity. Loop region mutations lead to a wide range of topologies, folding states, and altered physicochemical properties. A protein-folding study of Rop and several loop variants has identified specific residues and sequences that are linked to the observed structural plasticity. Apart from the native state, native-like and molten-globule states have been identified; these states are sensitive to reducing agents due to the formation of nonnative disulfide bridges. Pro residues in the loop are critical for the establishment of new topologies and molten globule states; their effects, however, can be in part compensated by Gly residues. The extreme plasticity in the assembly of 4-alpha-helical bundles reflects the capacity of the Rop sequence to combine a specific set of hydrophobic residues into strikingly different hydrophobic cores. These cores include highly hydrated ones that are consistent with the formation of interchain, nonnative disulfide bridges and the establishment of molten globules. Potential applications of this structural plasticity are among others in the engineering of bio-inspired materials.

Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.,Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Perez J, Kokkinidis M Proc Natl Acad Sci U S A. 2014 Jul 29;111(30):11049-54. doi:, 10.1073/pnas.1322065111. Epub 2014 Jul 14. PMID:25024213^[1]

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

References

↑ Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Perez J, Kokkinidis M. Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein. Proc Natl Acad Sci U S A. 2014 Jul 29;111(30):11049-54. doi:, 10.1073/pnas.1322065111. Epub 2014 Jul 14. PMID:25024213 doi:http://dx.doi.org/10.1073/pnas.1322065111

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4do2"

@@ Line 2: / Line 2: @@
 <StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4do2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DO2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4do2]] 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=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DO2 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rop|1rop]]</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 Escherichia coli])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [http://www.ebi.ac.uk/pdbsum/4do2 PDBsum]</span></td></tr>
 </table>
@@ Line 11: / Line 11: @@
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region has attracted considerable interest because a single alanine-to-proline substitution (A31P) in the loop is sufficient to change the topology of this small protein. In order to further analyse the loop region as a possible folding-control element, the double mutant D30P/A31G (RopPG) was produced, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 26.7, b = 38.8, c = 56.6 A, beta = 100.9 degrees and two molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 1.4 A using synchrotron radiation.
+The dimeric Repressor of Primer (Rop) protein, a widely used model system for the study of coiled-coil 4-alpha-helical bundles, is characterized by a remarkable structural plasticity. Loop region mutations lead to a wide range of topologies, folding states, and altered physicochemical properties. A protein-folding study of Rop and several loop variants has identified specific residues and sequences that are linked to the observed structural plasticity. Apart from the native state, native-like and molten-globule states have been identified; these states are sensitive to reducing agents due to the formation of nonnative disulfide bridges. Pro residues in the loop are critical for the establishment of new topologies and molten globule states; their effects, however, can be in part compensated by Gly residues. The extreme plasticity in the assembly of 4-alpha-helical bundles reflects the capacity of the Rop sequence to combine a specific set of hydrophobic residues into strikingly different hydrophobic cores. These cores include highly hydrated ones that are consistent with the formation of interchain, nonnative disulfide bridges and the establishment of molten globules. Potential applications of this structural plasticity are among others in the engineering of bio-inspired materials.
-Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.,Ambrazi M, Fellas G, Kapetaniou EG, Kotsifaki D, Providaki M, Kokkinidis M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):432-4. doi:, 10.1107/S1744309108011342. Epub 2008 Apr 30. PMID:18453719<ref>PMID:18453719</ref>
+Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.,Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Perez J, Kokkinidis M Proc Natl Acad Sci U S A. 2014 Jul 29;111(30):11049-54. doi:, 10.1073/pnas.1322065111. Epub 2014 Jul 14. PMID:25024213<ref>PMID:25024213</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
@@ Line 24: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Amprazi, M]]
 [[Category: Kapetaniou, E G]]
-[[Category: M., Kokkinidis]]
+[[Category: Kokkinidis, M]]
 [[Category: 4-alpha-helical bundle]]
 [[Category: Bacterial protein]]

4do2

From Proteopedia

Revision as of 09:33, 7 February 2015

Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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