2xpv
From Proteopedia
(Difference between revisions)
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<StructureSection load='2xpv' size='340' side='right' caption='[[2xpv]], [[Resolution|resolution]] 1.49Å' scene=''> | <StructureSection load='2xpv' size='340' side='right' caption='[[2xpv]], [[Resolution|resolution]] 1.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2xpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPV OCA]. <br> | + | <table><tr><td colspan='2'>[[2xpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XPV FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MIY:(4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE'>MIY</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MIY:(4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE'>MIY</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xgc|2xgc]], [[2xpw|2xpw]], [[3zqg|3zqg]], [[2x9d|2x9d]], [[1bjz|1bjz]], [[3zqh|3zqh]], [[2trt|2trt]], [[2vkv|2vkv]], [[1ork|1ork]], [[2xge|2xge]], [[1a6i|1a6i]], [[2x6o|2x6o]], [[1qpi|1qpi]], [[2vke|2vke]], [[1du7|1du7]], [[2xgd|2xgd]], [[2xrl|2xrl]], [[2xpt|2xpt]], [[2xpu|2xpu]], [[2xb5|2xb5]], [[3zqf|3zqf]], [[3zqi|3zqi]], [[1bj0|1bj0]], [[2xps|2xps]], [[1bjy|1bjy]], [[2tct|2tct]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xgc|2xgc]], [[2xpw|2xpw]], [[3zqg|3zqg]], [[2x9d|2x9d]], [[1bjz|1bjz]], [[3zqh|3zqh]], [[2trt|2trt]], [[2vkv|2vkv]], [[1ork|1ork]], [[2xge|2xge]], [[1a6i|1a6i]], [[2x6o|2x6o]], [[1qpi|1qpi]], [[2vke|2vke]], [[1du7|1du7]], [[2xgd|2xgd]], [[2xrl|2xrl]], [[2xpt|2xpt]], [[2xpu|2xpu]], [[2xb5|2xb5]], [[3zqf|3zqf]], [[3zqi|3zqi]], [[1bj0|1bj0]], [[2xps|2xps]], [[1bjy|1bjy]], [[2tct|2tct]]</td></tr> |
| - | <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=2xpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xpv RCSB], [http://www.ebi.ac.uk/pdbsum/2xpv PDBsum]</span></td></tr> |
| - | + | </table> | |
| - | <table> | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/TETR4_ECOLX TETR4_ECOLX]] TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.,Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W Science. 1994 Apr 15;264(5157):418-20. PMID:8153629<ref>PMID:8153629</ref> | Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.,Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W Science. 1994 Apr 15;264(5157):418-20. PMID:8153629<ref>PMID:8153629</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Tetracycline repressor protein|Tetracycline repressor protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Dalm, D | + | [[Category: Dalm, D]] |
| - | [[Category: Hinrichs, W | + | [[Category: Hinrichs, W]] |
| - | [[Category: Palm, G J | + | [[Category: Palm, G J]] |
| - | [[Category: Proft, J | + | [[Category: Proft, J]] |
[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
[[Category: Metal coordination]] | [[Category: Metal coordination]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription regulator]] | [[Category: Transcription regulator]] | ||
Revision as of 18:43, 24 December 2014
TETR(D) IN COMPLEX WITH MINOCYCLINE AND MAGNESIUM.
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