1i1g: Difference between revisions
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<StructureSection load='1i1g' size='340' side='right' caption='[[1i1g]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1i1g' size='340' side='right' caption='[[1i1g]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1i1g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <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://oca.weizmann.ac.il/oca-docs/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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i1g RCSB], [http://www.ebi.ac.uk/pdbsum/1i1g PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1i1g" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 43587]] | ||
[[Category: Brinkman, A B]] | [[Category: Brinkman, A B]] | ||
[[Category: Leonard, P M]] | [[Category: Leonard, P M]] | ||
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[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
[[Category: Lrp/asnc family]] | [[Category: Lrp/asnc family]] | ||
[[Category: Pyrococcus furiosus]] | |||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcriptional regulator]] | [[Category: Transcriptional regulator]] | ||
Revision as of 03:01, 11 September 2015
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
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. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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