2bsq: Difference between revisions

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<StructureSection load='2bsq' size='340' side='right'caption='[[2bsq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='2bsq' size='340' side='right'caption='[[2bsq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bsq]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus gonorrhoeae" (zopf 1885) lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bsq]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSQ FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5IU:5-IODO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>5IU</scene></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]] 3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yh4|1yh4]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5IU:5-IODO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>5IU</scene></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=2bsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsq OCA], [https://pdbe.org/2bsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsq RCSB], [https://www.ebi.ac.uk/pdbsum/2bsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsq 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=2bsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsq OCA], [https://pdbe.org/2bsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsq RCSB], [https://www.ebi.ac.uk/pdbsum/2bsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1]] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. [[https://www.uniprot.org/uniprot/FITA_NEIG1 FITA_NEIG1]] Antitoxin component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.<ref>PMID:10639460</ref> 
[https://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Brennan, R G]]
[[Category: Neisseria gonorrhoeae]]
[[Category: Mattison, K]]
[[Category: Brennan RG]]
[[Category: So, M]]
[[Category: Mattison K]]
[[Category: Wilbur, J S]]
[[Category: So M]]
[[Category: Dna binding]]
[[Category: Wilbur JS]]
[[Category: Heterodimer]]
[[Category: Pin domain]]
[[Category: Ribbon-helix-helix]]
[[Category: Transcription]]
[[Category: Transcription regulation complex]]
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