1i1g: Difference between revisions

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[[Image:1i1g.gif|left|200px]]


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==CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS==
The line below this paragraph, containing "STRUCTURE_1i1g", creates the "Structure Box" on the page.
<StructureSection load='1i1g' size='340' side='right'caption='[[1i1g]], [[Resolution|resolution]] 2.90&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'>[[1i1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1G 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]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1g OCA], [https://pdbe.org/1i1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1g RCSB], [https://www.ebi.ac.uk/pdbsum/1i1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1g ProSAT]</span></td></tr>
{{STRUCTURE_1i1g|  PDB=1i1g |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/REG7_PYRFU REG7_PYRFU] Negatively regulates its own transcription. Binds to a 46-base pair sequence that overlaps the transcriptional start site of its own promoter.
== 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/i1/1i1g_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=1i1g ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS'''
==See Also==
 
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 A resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel beta-sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled to mutational analysis.
[[Category: Large Structures]]
 
==About this Structure==
1I1G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1G OCA].
 
==Reference==
Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus., Leonard PM, Smits SH, Sedelnikova SE, Brinkman AB, de Vos WM, van der Oost J, Rice DW, Rafferty JB, EMBO J. 2001 Mar 1;20(5):990-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11230123 11230123]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Brinkman, A B.]]
[[Category: Leonard, P M.]]
[[Category: Oost, J van der.]]
[[Category: Rafferty, J B.]]
[[Category: Rice, D W.]]
[[Category: Sedelnikova, S E.]]
[[Category: Smits, S H.J.]]
[[Category: Vos, W M.de.]]
[[Category: Helix-turn-helix]]
[[Category: Lrp/asnc family]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Transcriptional regulator]]
[[Category: Brinkman AB]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:27:44 2008''
[[Category: Leonard PM]]
[[Category: Rafferty JB]]
[[Category: Rice DW]]
[[Category: Sedelnikova SE]]
[[Category: Smits SHJ]]
[[Category: De Vos WM]]
[[Category: Van der Oost J]]

Latest revision as of 10:31, 7 February 2024

CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUSCRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS

Structural highlights

1i1g is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

REG7_PYRFU Negatively regulates its own transcription. Binds to a 46-base pair sequence that overlaps the transcriptional start site of its own promoter.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1i1g, resolution 2.90Å

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