1uxc: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
Line 1: Line 1:


==FRUCTOSE REPRESSOR DNA-BINDING DOMAIN, NMR, MINIMIZED STRUCTURE==
==FRUCTOSE REPRESSOR DNA-BINDING DOMAIN, NMR, MINIMIZED STRUCTURE==
<StructureSection load='1uxc' size='340' side='right'caption='[[1uxc]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1uxc' size='340' side='right'caption='[[1uxc]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1uxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UXC FirstGlance]. <br>
<table><tr><td colspan='2'>[[1uxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UXC FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uxd|1uxd]]</div></td></tr>
</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=1uxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uxc OCA], [https://pdbe.org/1uxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uxc RCSB], [https://www.ebi.ac.uk/pdbsum/1uxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uxc ProSAT]</span></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=1uxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uxc OCA], [https://pdbe.org/1uxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uxc RCSB], [https://www.ebi.ac.uk/pdbsum/1uxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uxc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CRA_ECOLI CRA_ECOLI]] Global transcriptional regulator, which plays an important role in the regulation of carbon metabolism. Activates transcription of genes encoding biosynthetic and oxidative enzymes (involved in Krebs cycle, glyoxylate shunt and gluconeogenesis, such as ppsA and fbp). Represses genes involved in sugar catabolism, such as fruB, pfkA, pykF and adhE. Binds asymmetrically to the two half-sites of its operator.<ref>PMID:16115199</ref> <ref>PMID:8195118</ref> <ref>PMID:8230205</ref> <ref>PMID:8550429</ref> <ref>PMID:8577250</ref> <ref>PMID:8858581</ref> <ref>PMID:9084760</ref> <ref>PMID:9371462</ref>
[https://www.uniprot.org/uniprot/CRA_ECOLI CRA_ECOLI] Global transcriptional regulator, which plays an important role in the regulation of carbon metabolism. Activates transcription of genes encoding biosynthetic and oxidative enzymes (involved in Krebs cycle, glyoxylate shunt and gluconeogenesis, such as ppsA and fbp). Represses genes involved in sugar catabolism, such as fruB, pfkA, pykF and adhE. Binds asymmetrically to the two half-sites of its operator.<ref>PMID:16115199</ref> <ref>PMID:8195118</ref> <ref>PMID:8230205</ref> <ref>PMID:8550429</ref> <ref>PMID:8577250</ref> <ref>PMID:8858581</ref> <ref>PMID:9084760</ref> <ref>PMID:9371462</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</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=1uxc 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=1uxc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
FruR is an Escherichia coli transcriptional regulator that belongs to the LacI DNA-binding protein family. By using 1H and 15N NMR spectroscopy, we have determined the three-dimensional solution structure of the FruR N-terminal DNA-binding domain consisting of 57 amino acid residues. A total of 809 NMR-derived distances and 54 dihedral angle constraints have been used for molecular modelling with the X-PLOR program. The resulting set of calculated structures presents an average root-mean-square deviation of 0.37 A at the main-chain level for the first 47 residues. This highly defined N-terminal part of the structure reveals a similar topology for the three alpha-helices when compared to the 3D structures of LacI and PurR counterparts. The most striking difference lies in the connection between helix II and helix III, in which three additional residues are present in FruR. This connecting segment is well structured and contains a type III turn. Apart from hydrophobic interactions of non-polar residues with the core of the domain, this connecting segment is stabilised by several hydrogen bonds and by the aromatic ring stacking between Tyr19 of helix II and Tyr28 of the turn. The region containing the putative "hinge helix" (helix IV), that has been described in PurR-DNA complex to make specific base contacts in the minor groove of DNA, is unfolded. Examination of hydrogen bonds highlights the importance of homologous residues that seem to be conserved for their ability to fulfill helix N and C-capping roles in the LacI repressor family.
Three-dimensional structure of the DNA-binding domain of the fructose repressor from Escherichia coli by 1H and 15N NMR.,Penin F, Geourjon C, Montserret R, Bockmann A, Lesage A, Yang YS, Bonod-Bidaud C, Cortay JC, Negre D, Cozzone AJ, Deleage G J Mol Biol. 1997 Jul 18;270(3):496-510. PMID:9237914<ref>PMID:9237914</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1uxc" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bockmann, A]]
[[Category: Bockmann A]]
[[Category: Bonod-Bidaud, C]]
[[Category: Bonod-Bidaud C]]
[[Category: Cortay, J C]]
[[Category: Cortay JC]]
[[Category: Cozzone, A J]]
[[Category: Cozzone AJ]]
[[Category: Deleage, G]]
[[Category: Deleage G]]
[[Category: Geourjon, C]]
[[Category: Geourjon C]]
[[Category: Lesage, A]]
[[Category: Lesage A]]
[[Category: Montserret, R]]
[[Category: Montserret R]]
[[Category: Negre, D]]
[[Category: Negre D]]
[[Category: Penin, F]]
[[Category: Penin F]]
[[Category: Yang, Y]]
[[Category: Yang Y]]
[[Category: Dna-binding protein]]
[[Category: Fructose repressor]]
[[Category: Laci family]]
[[Category: Transcription regulation]]
Retrieved from "https://proteopedia.org/1uxc"