1k67: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1k67.png|left|200px]]
-<!--
+==MODEL INTERACTION BETWEEN BIRA AND BCCP==
-The line below this paragraph, containing "STRUCTURE_1k67", creates the "Structure Box" on the page.
+<StructureSection load='1k67' size='340' side='right'caption='[[1k67]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K67 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1k67 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1k67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k67 ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1k67|  PDB=1k67  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier protein to which BirA transfers biotin. The model is consistent with prior physical and biochemical studies. Measurement of transfer rates for variants of BirA with single-site mutations in the proposed BirA:BCCP interface region also provides support. The unique feature of the proposed interaction between BirA and BCCP is that it uses the same beta-sheet region on the surface of BirA that the protein uses for homodimerization into a form competent to bind DNA. The resulting mutually exclusive protein:protein interfaces explain the novel feature of the BirA regulatory system, namely, that transcription of the genes involved in biotin synthesis is not determined by the level of biotin, per se, but by the level of unmodified BCCP. The model also provides a role for the C-terminal domain of BirA that is structurally similar to an SH3 domain.
-===MODEL INTERACTION BETWEEN BIRA AND BCCP===
+Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.,Weaver LH, Kwon K, Beckett D, Matthews BW Protein Sci. 2001 Dec;10(12):2618-22. PMID:11714930<ref>PMID:11714930</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11714930}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1k67" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11714930 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11714930}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K67 OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:11714930</ref><references group="xtra"/>
 [[Category: Beckett, D]]
 [[Category: Kwon, K]]
 [[Category: Matthews, B W]]
 [[Category: Weaver, L H]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:49:36 2010''