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1iz1

From Proteopedia

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CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR

Structural highlights

1iz1 is a 4 chain structure with sequence from Cupriavidus necator. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9WXC7_CUPNE

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 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.

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^[1]

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

References

↑ Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T. 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. J Mol Biol. 2003 May 2;328(3):555-66. PMID:12706716

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/1iz1"

@@ Line 3: / Line 3: @@
 <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/Atcc_43291 Atcc 43291]. 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>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ixc|1ixc]]</div></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]] 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]]
@@ Line 26: / Line 28: @@
 </div>
 <div class="pdbe-citations 1iz1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43291]]
+[[Category: Cupriavidus necator]]
 [[Category: Large Structures]]
-[[Category: Miyashita, K]]
+[[Category: Miyashita K]]
-[[Category: Muraoka, S]]
+[[Category: Muraoka S]]
-[[Category: Ogawa, N]]
+[[Category: Ogawa N]]
-[[Category: Okumura, R]]
+[[Category: Okumura R]]
-[[Category: Senda, T]]
+[[Category: Senda T]]
-[[Category: Dna binding protein]]
-[[Category: Long alpha helix connecting dna binding and regulatory domain]]

1iz1

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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