1ufr: Difference between revisions

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<StructureSection load='1ufr' size='340' side='right' caption='[[1ufr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1ufr' size='340' side='right' caption='[[1ufr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ufr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UFR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ufr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UFR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1ufr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ufr RCSB], [http://www.ebi.ac.uk/pdbsum/1ufr PDBsum], [http://www.topsan.org/Proteins/RSGI/1ufr TOPSAN]</span></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=1ufr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufr OCA], [http://pdbe.org/1ufr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ufr RCSB], [http://www.ebi.ac.uk/pdbsum/1ufr PDBsum], [http://www.topsan.org/Proteins/RSGI/1ufr TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Thermus thermophilus]]
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Kuramitsu, S]]
[[Category: Kuramitsu, S]]
[[Category: Matsuura, T]]
[[Category: Matsuura, T]]

Revision as of 18:03, 11 September 2015

Crystal Structure of TT1027 from Thermus thermophilus HB8Crystal Structure of TT1027 from Thermus thermophilus HB8

Structural highlights

1ufr is a 4 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

Function

[PYRR_THET8] Probably regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines. In contrast to pyr attenuation in Bacillus, PyrR from Thermus could act as a translational repressor: the binding of PyrR at its proposed recognition site in the transcript would prevent initiation of translation of the leader peptide, resulting in terminator formation and reduced expression of downstream genes (By similarity). Also displays uracil phosphoribosyltransferase activity (By similarity).

Evolutionary Conservation

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

1ufr, resolution 2.60Å

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