3qop
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qop]] is a 2 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=3QOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QOP FirstGlance]. <br> | <table><tr><td colspan='2'>[[3qop]] is a 2 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=3QOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QOP FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i5z|1i5z]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i5z|1i5z]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crp, cap, csm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crp, cap, csm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qop OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qop RCSB], [http://www.ebi.ac.uk/pdbsum/3qop PDBsum]</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=3qop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qop OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qop RCSB], [http://www.ebi.ac.uk/pdbsum/3qop PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution.,Weber IT, Steitz TA J Mol Biol. 1987 Nov 20;198(2):311-26. PMID:2828639<ref>PMID:2828639</ref> | Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution.,Weber IT, Steitz TA J Mol Biol. 1987 Nov 20;198(2):311-26. PMID:2828639<ref>PMID:2828639</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Knapp, J | + | [[Category: Knapp, J]] |
| - | [[Category: Lee, J C | + | [[Category: Lee, J C]] |
| - | [[Category: White, M A | + | [[Category: White, M A]] |
[[Category: Allostery]] | [[Category: Allostery]] | ||
[[Category: Dna binding cyclic amp]] | [[Category: Dna binding cyclic amp]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
Revision as of 21:35, 3 January 2015
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
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