1qx8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:57, 23 August 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1qx8.png|left|200px]]
 
-
<!--
+
==Crystal structure of a five-residue deletion mutant of the Rop protein==
-
The line below this paragraph, containing "STRUCTURE_1qx8", creates the "Structure Box" on the page.
+
<StructureSection load='1qx8' size='340' side='right'caption='[[1qx8]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1qx8]] 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=1QX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QX8 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</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=1qx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx8 OCA], [https://pdbe.org/1qx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qx8 RCSB], [https://www.ebi.ac.uk/pdbsum/1qx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx8 ProSAT]</span></td></tr>
-
{{STRUCTURE_1qx8| PDB=1qx8 | SCENE= }}
+
</table>
 +
== 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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qx8_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qx8 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The repressor of primer (Rop) protein has become a steady source of surprises concerning the relationship between the sequences and the structures of several of its mutants and variants. Here we add another piece to the puzzle of Rop by showing that an engineered deletion mutant of the protein (corresponding to a deletion of residues 30-34 of the wild-type protein and designed to restore the heptad periodicity at the turn region) results in a complete reorganization of the bundle which is converted from a homodimer to a homotetramer. In contrast (and as previously shown), a two-residue insertion, which also restores the heptad periodicity, is essentially identical with wild-type Rop. The new deletion mutant structure is a canonical, left-handed, all-antiparallel bundle with a completely different hydrophobic core and distinct surface properties. The structure agrees and qualitatively explains the results from functional, thermodynamic, and kinetic studies which indicated that this deletion mutant is a biologically inactive hyperstable homotetramer. Additional insight into the stability and dynamics of the mutant structure has been obtained from extensive molecular dynamics simulations in explicit water and with full treatment of electrostatics.
-
===Crystal structure of a five-residue deletion mutant of the Rop protein===
+
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein.,Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:16953576<ref>PMID:16953576</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1qx8" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_16953576}}, adds the Publication Abstract to the page
+
*[[Rop protein|Rop protein]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 16953576 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16953576}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1QX8 is a [[Single protein]] structure of 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=1QX8 OCA].
+
-
 
+
-
==Reference==
+
-
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein., Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M, Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16953576 16953576]
+
-
 
+
-
Ionic strength reducers: an efficient approach to protein purification and crystallization. Application to two Rop variants., Papanikolau Y, Kotsifaki D, Fadouloglou VE, Gazi AD, Glykos NM, Cesareni G, Kokkinidis M, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1334-7. Epub 2004, Jun 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15213408 15213408]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Cesareni, G.]]
+
[[Category: Cesareni G]]
-
[[Category: Glykos, N M.]]
+
[[Category: Glykos NM]]
-
[[Category: Kokkinidis, M.]]
+
[[Category: Kokkinidis M]]
-
[[Category: Kotsifaki, D.]]
+
[[Category: Kotsifaki D]]
-
[[Category: Papanikolaou, Y.]]
+
[[Category: Papanikolaou Y]]
-
[[Category: Vlassi, M.]]
+
[[Category: Vlassi M]]
-
[[Category: Initiation of transcription]]
+
-
[[Category: Replication]]
+
-
[[Category: Rna primer]]
+
-
[[Category: X-ray]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:53:37 2008''
+

Current revision

Crystal structure of a five-residue deletion mutant of the Rop protein

PDB ID 1qx8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qx8"
Personal tools