4l51: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4l51|  PDB=4l51  |  SCENE=  }}
===Crystal structures of the LsrR proteins complexed with phospho-AI-2 and its two different analogs reveal distinct mechanisms for ligand recognition===
{{ABSTRACT_PUBMED_24047255}}


==Function==
==Crystal structures of the LsrR proteins complexed with phospho-AI-2 and its two different analogs reveal distinct mechanisms for ligand recognition==
[[http://www.uniprot.org/uniprot/LSRR_ECOLI LSRR_ECOLI]] Regulates transcription of many different genes. In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFG operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes.<ref>PMID:15601708</ref> <ref>PMID:15743955</ref> <ref>PMID:17557827</ref>
<StructureSection load='4l51' size='340' side='right'caption='[[4l51]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4l51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L51 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSX:5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE'>HSX</scene></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=4l51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l51 OCA], [https://pdbe.org/4l51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l51 RCSB], [https://www.ebi.ac.uk/pdbsum/4l51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l51 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LSRR_ECOLI LSRR_ECOLI] Regulates transcription of many different genes. In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFG operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes.<ref>PMID:15601708</ref> <ref>PMID:15743955</ref> <ref>PMID:17557827</ref>  


==About this Structure==
==See Also==
[[4l51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L51 OCA].
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024047255</ref><references group="xtra"/><references/>
__TOC__
[[Category: Escherichia coli k-12]]
</StructureSection>
[[Category: Eo, Y.]]
[[Category: Escherichia coli K-12]]
[[Category: Ha, J H.]]
[[Category: Large Structures]]
[[Category: Ryu, K S.]]
[[Category: Eo Y]]
[[Category: Dna binding]]
[[Category: Ha JH]]
[[Category: Dna transcriptional regulator]]
[[Category: Ryu KS]]
[[Category: Phospho-ai-2 binding]]
[[Category: Removed helix-turn-helix domain]]
[[Category: Sorc/deor family]]
[[Category: Transcription regulator]]

Latest revision as of 12:17, 1 March 2024

Crystal structures of the LsrR proteins complexed with phospho-AI-2 and its two different analogs reveal distinct mechanisms for ligand recognition

4l51, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA