1i1g: Difference between revisions

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<StructureSection load='1i1g' size='340' side='right'caption='[[1i1g]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1i1g' size='340' side='right'caption='[[1i1g]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1i1g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1I1G FirstGlance]. <br>
<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>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1i1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1g OCA], [http://pdbe.org/1i1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i1g RCSB], [http://www.ebi.ac.uk/pdbsum/1i1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1g ProSAT]</span></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]] 2.9&#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=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>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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:11230123<ref>PMID:11230123</ref>
==See Also==
 
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i1g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43587]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[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: Transcription]]
[[Category: Brinkman AB]]
[[Category: Transcriptional regulator]]
[[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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OCA
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