1iz1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1iz1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iz1, resolution 2.50&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Current revision (07:13, 25 October 2023) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1iz1.jpg|left|200px]]<br /><applet load="1iz1" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1iz1, resolution 2.50&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR==
-
The LysR-type transcriptional regulator (LTTR) proteins are one of the, most common transcriptional regulators in prokaryotes. Here we report the, crystal structure of CbnR, which is one of the LTTRs derived from, Ralstonia eutropha NH9. This is the first crystal structure of a, full-length LTTR. CbnR was found to form a homo-tetramer, which seems to, be a biologically active form. Surprisingly, the tetramer can be regarded, as a dimer of dimers, whereby each dimer is composed of two subunits in, different conformations. In the CbnR tetramer, the DNA-binding domains are, located at the V-shaped bottom of the main body of the tetramer, and seem, to be suitable to interact with a long stretch of the promoter DNA, which, is approximately 60bp. Interaction between the four DNA-binding domains, and the two binding sites on the target DNA is likely to bend the target, DNA along the V-shaped bottom of the CbnR tetramer. The relaxation of the, bent DNA, which occurs upon inducer binding to CbnR, seems to be, associated with a quaternary structure change of the tetramer.
+
<StructureSection load='1iz1' size='340' side='right'caption='[[1iz1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1iz1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IZ1 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=1iz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz1 OCA], [https://pdbe.org/1iz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iz1 RCSB], [https://www.ebi.ac.uk/pdbsum/1iz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iz1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9WXC7_CUPNE Q9WXC7_CUPNE]
 +
== 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/iz/1iz1_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=1iz1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The LysR-type transcriptional regulator (LTTR) proteins are one of the most common transcriptional regulators in prokaryotes. Here we report the crystal structure of CbnR, which is one of the LTTRs derived from Ralstonia eutropha NH9. This is the first crystal structure of a full-length LTTR. CbnR was found to form a homo-tetramer, which seems to be a biologically active form. Surprisingly, the tetramer can be regarded as a dimer of dimers, whereby each dimer is composed of two subunits in different conformations. In the CbnR tetramer, the DNA-binding domains are located at the V-shaped bottom of the main body of the tetramer, and seem to be suitable to interact with a long stretch of the promoter DNA, which is approximately 60bp. Interaction between the four DNA-binding domains and the two binding sites on the target DNA is likely to bend the target DNA along the V-shaped bottom of the CbnR tetramer. The relaxation of the bent DNA, which occurs upon inducer binding to CbnR, seems to be associated with a quaternary structure change of the tetramer.
-
==About this Structure==
+
Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend.,Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T J Mol Biol. 2003 May 2;328(3):555-66. PMID:12706716<ref>PMID:12706716</ref>
-
1IZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IZ1 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend., Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T, J Mol Biol. 2003 May 2;328(3):555-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12706716 12706716]
+
</div>
-
[[Category: Cupriavidus necator]]
+
<div class="pdbe-citations 1iz1" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Miyashita, K.]]
+
-
[[Category: Muraoka, S.]]
+
-
[[Category: Ogawa, N.]]
+
-
[[Category: Okumura, R.]]
+
-
[[Category: Senda, T.]]
+
-
[[Category: long alpha helix connecting dna binding and regulatory domains]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:49:10 2007''
+
==See Also==
 +
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Cupriavidus necator]]
 +
[[Category: Large Structures]]
 +
[[Category: Miyashita K]]
 +
[[Category: Muraoka S]]
 +
[[Category: Ogawa N]]
 +
[[Category: Okumura R]]
 +
[[Category: Senda T]]

Current revision

CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR

PDB ID 1iz1

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/1iz1"
Personal tools