This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lr1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:47, 22 May 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1lr1.png|left|200px]]
 
-
<!--
+
==Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS==
-
The line below this paragraph, containing "STRUCTURE_1lr1", creates the "Structure Box" on the page.
+
<StructureSection load='1lr1' size='340' side='right'caption='[[1lr1]]' 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'>[[1lr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LR1 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">Solution NMR</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=1lr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lr1 OCA], [https://pdbe.org/1lr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lr1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lr1 ProSAT]</span></td></tr>
-
{{STRUCTURE_1lr1| PDB=1lr1 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HNS_ECOLI HNS_ECOLI] A DNA-binding protein implicated in transcriptional repression (silencing) as well as in bacterial chromosome organization. H-NS binds tightly to AT-rich dsDNA, increases its thermal stability and inhibits transcription. Also binds to ssDNA and RNA but with a much lower affinity. H-NS has possible histone-like function. May be a global transcriptional regulator through its ability to bind to curved DNA sequences, which are found in regions upstream of a certain subset of promoters. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its role is antagonized by LeuO. Subject to transcriptional auto-repression. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150.<ref>PMID:7934818</ref> <ref>PMID:11031114</ref> <ref>PMID:17010156</ref> <ref>PMID:20659289</ref>
 +
== 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/lr/1lr1_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=1lr1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
H-NS plays a role in condensing DNA in the bacterial nucleoid. This 136 amino acid protein comprises two functional domains separated by a flexible linker. High order structures formed by the N-terminal oligomerization domain (residues 1-89) constitute the basis of a protein scaffold that binds DNA via the C-terminal domain. Deletion of residues 57-89 or 64-89 of the oligomerization domain precludes high order structure formation, yielding a discrete dimer. This dimerization event represents the initial event in the formation of high order structure. The dimers thus constitute the basic building block of the protein scaffold. The three-dimensional solution structure of one of these units (residues 1-57) has been determined. Activity of these structural units is demonstrated by a dominant negative effect on high order structure formation on addition to the full length protein. Truncated and site-directed mutant forms of the N-terminal domain of H-NS reveal how the dimeric unit self-associates in a head-to-tail manner and demonstrate the importance of secondary structure in this interaction to form high order structures. A model is presented for the structural basis for DNA packaging in bacterial cells.
-
===Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS===
+
H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein.,Esposito D, Petrovic A, Harris R, Ono S, Eccleston JF, Mbabaali A, Haq I, Higgins CF, Hinton JC, Driscoll PC, Ladbury JE J Mol Biol. 2002 Dec 6;324(4):841-50. PMID:12460581<ref>PMID:12460581</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_12460581}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1lr1" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 12460581 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_12460581}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1LR1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR1 OCA].
+
-
 
+
-
==Reference==
+
-
H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein., Esposito D, Petrovic A, Harris R, Ono S, Eccleston JF, Mbabaali A, Haq I, Higgins CF, Hinton JC, Driscoll PC, Ladbury JE, J Mol Biol. 2002 Dec 6;324(4):841-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12460581 12460581]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Driscoll, P C.]]
+
[[Category: Driscoll PC]]
-
[[Category: Eccleston, J.]]
+
[[Category: Eccleston J]]
-
[[Category: Esposito, D.]]
+
[[Category: Esposito D]]
-
[[Category: Haq, I.]]
+
[[Category: Haq I]]
-
[[Category: Harris, R.]]
+
[[Category: Harris R]]
-
[[Category: Higgins, C F.]]
+
[[Category: Higgins CF]]
-
[[Category: Hinton, J C.D.]]
+
[[Category: Hinton JCD]]
-
[[Category: Ladbury, J E.]]
+
[[Category: Ladbury JE]]
-
[[Category: Mbabaali, A.]]
+
[[Category: Mbabaali A]]
-
[[Category: Ono, S.]]
+
[[Category: Ono S]]
-
[[Category: Petrovic, A.]]
+
[[Category: Petrovic A]]
-
[[Category: Chromatin]]
+
-
[[Category: Coiled-coil]]
+
-
[[Category: Dna packaging]]
+
-
[[Category: Nucleoid assembly]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:50:24 2008''
+

Current revision

Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS

PDB ID 1lr1

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/1lr1"
Personal tools