4do2 - Revision history

OCA at 14:40, 14 March 2024

2024-03-14T14:40:12Z

←Older revision		Revision as of 14:40, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4do2]] 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=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DO2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4do2]] 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=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DO2 FirstGlance]. <br>
-	</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=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [https://pdbe.org/4do2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [https://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 ProSAT]</span></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]] 1.401Å</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=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [https://pdbe.org/4do2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [https://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 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.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== 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<ref>PMID:25024213</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4do2" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Rop protein\|Rop protein]]		*[[Rop protein\|Rop protein]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:31, 21 September 2022

2022-09-21T08:31:33Z

←Older revision		Revision as of 08:31, 21 September 2022
Line 1:		Line 1:

	==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==		==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==
-	<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' scene=''>	+	<StructureSection load='4do2' size='340' side='right'caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<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>	+	<table><tr><td colspan='2'>[[4do2]] 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=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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>~~	+	</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=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [https://pdbe.org/4do2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [https://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 ProSAT]</span></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~~://pdbe.org/4do2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
-	[[Category: ~~Amprazi, M~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Kapetaniou, E G]]~~	+	[[Category: Amprazi M]]
-	~~[[Category: Kokkinidis,~~ M]]	+	[[Category: Kapetaniou EG]]
-	[[Category: ~~4-alpha-helical bundle~~]]	+	[[Category: Kokkinidis M]]
-	[[Category: ~~Bacterial protein]]~~	+
-	~~[[Category: Cole1 plasmid copy number]]~~	+
-	~~[[Category: Loop]]~~	+
-	~~[[Category: Mutation]]~~	+
-	~~[[Category: Protein folding]]~~	+
-	~~[[Category: Protein structure]]~~	+
-	~~[[Category: Rna binding protein]]~~	+
-	~~[[Category: Rop protein~~]]	+

OCA at 21:00, 11 August 2016

2016-08-11T21:00:02Z

←Older revision		Revision as of 21:00, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==		==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==
	<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' scene=''>
Line 5:		Line 6:
	</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='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 "Bacillus coli" Migula 1895])</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>	+	<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://pdbe.org/4do2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [http://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4do2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 09:33, 7 February 2015

2015-02-07T09:33:23Z

←Older revision		Revision as of 09:33, 7 February 2015
Line 2:		Line 2:
	<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== 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>		</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>		<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>		</table>
Line 11:		Line 11:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Amprazi, M]]		[[Category: Amprazi, M]]
	[[Category: Kapetaniou, E G]]		[[Category: Kapetaniou, E G]]
-	[[Category: ~~M.,~~ Kokkinidis]]	+	[[Category: Kokkinidis, M]]
	[[Category: 4-alpha-helical bundle]]		[[Category: 4-alpha-helical bundle]]
	[[Category: Bacterial protein]]		[[Category: Bacterial protein]]

OCA at 22:39, 25 December 2014

2014-12-25T22:39:33Z

←Older revision		Revision as of 22:39, 25 December 2014
Line 7:		Line 7:
	<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>		<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>		</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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:13, 9 December 2014

2014-12-09T17:13:49Z

←Older revision		Revision as of 17:13, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4do2.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==
		+	<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution\|resolution]] 1.40Å' 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>
		+	</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='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>
		+	<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.

-	~~{{STRUCTURE_4do2\| PDB=4do2 \| SCENE= }}~~	+	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>

-	~~===Crystal Structure~~ of the ~~Rop protein mutant D30P/A31G at resolution 1~~.~~4 resolution~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_18453719}}~~	+	==See Also==
-		+	*[[Rop protein\|Rop protein]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~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].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Amprazi, M.]]	+	[[Category: Amprazi, M]]
-	[[Category: Kapetaniou, E G.]]	+	[[Category: Kapetaniou, E G]]
-	[[Category: M., Kokkinidis.]]	+	[[Category: M., Kokkinidis]]
	[[Category: 4-alpha-helical bundle]]		[[Category: 4-alpha-helical bundle]]
	[[Category: Bacterial protein]]		[[Category: Bacterial protein]]

OCA at 10:40, 13 February 2013

2013-02-13T10:40:15Z

←Older revision		Revision as of 10:40, 13 February 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4do2.jpg\|left\|200px]]

-	~~The entry~~ 4do2 ~~is ON HOLD~~ ~~until Feb 09 2014~~	+	{{STRUCTURE_4do2\| PDB=4do2 \| SCENE= }}

-	~~Authors: Amprazi, M~~.~~, Kapetaniou, E.G., Kokkinidis M~~.	+	===Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.===

-	~~Description: Crystal~~ Structure ~~of the Rop protein mutant D30P~~/~~A31G at resolution 1~~.~~4 resolution~~.	+	{{ABSTRACT_PUBMED_18453719}}
		+
		+	==About this Structure==
		+	[[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].
		+	[[Category: Escherichia coli]]
		+	[[Category: Amprazi, M.]]
		+	[[Category: Kapetaniou, E G.]]
		+	[[Category: M., Kokkinidis.]]
		+	[[Category: 4-alpha-helical bundle]]
		+	[[Category: Bacterial protein]]
		+	[[Category: Cole1 plasmid copy number]]
		+	[[Category: Loop]]
		+	[[Category: Mutation]]
		+	[[Category: Protein folding]]
		+	[[Category: Protein structure]]
		+	[[Category: Rna binding protein]]
		+	[[Category: Rop protein]]

OCA at 07:30, 22 February 2012

2012-02-22T07:30:39Z

←Older revision		Revision as of 07:30, 22 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4do2 is ON HOLD	+	The entry 4do2 is ON HOLD until Feb 09 2014

	Authors: Amprazi, M., Kapetaniou, E.G., Kokkinidis M.		Authors: Amprazi, M., Kapetaniou, E.G., Kokkinidis M.

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

OCA: Protected "4do2" [edit=sysop:move=sysop]

2012-02-15T06:26:14Z

Protected "4do2" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:26, 15 February 2012

OCA: New page: '''Unreleased structure''' The entry 4do2 is ON HOLD Authors: Amprazi, M., Kapetaniou, E.G., Kokkinidis M. Description: Crystal Structure of the Rop protein mutant D30P/A31G at resolut...

2012-02-15T06:26:13Z

New page: '''Unreleased structure''' The entry 4do2 is ON HOLD Authors: Amprazi, M., Kapetaniou, E.G., Kokkinidis M. Description: Crystal Structure of the Rop protein mutant D30P/A31G at resolut...

New page

'''Unreleased structure'''

The entry 4do2 is ON HOLD

Authors: Amprazi, M., Kapetaniou, E.G., Kokkinidis M.

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