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< | ==MODEL OF LACTOSE REPRESSOR CORE BASED ON ALIGNMENT WITH SUGAR BINDING PROTEINS IS CONCORDANT WITH GENETIC AND CHEMICAL DATA== | ||
<StructureSection load='1ltp' size='340' side='right'caption='[[1ltp]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTP FirstGlance]. <br> | |||
</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=1ltp FirstGlance], [https://www.ebi.ac.uk/pdbsum/1ltp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Using primary sequence similarity to arabinose-binding protein, D-glucose/D-galactose-binding protein, and ribose-binding protein (Vyas, N. K., Vyas, M. N., and Quiocho, F. A. (1991) J. Biol. Chem. 266, 5226-5237; Mowbray, S. L., and Cole, L. B. (1992) J. Mol. Biol. 225, 155-175), the core domain (residues 62-323) of the bacterial regulatory protein lac repressor has been aligned to these sugar-binding proteins of known structure. Although the sequence identity is not striking, there is strong overall homology based on two separate matrix scoring systems (minimum base change per codon (MBC/C) and amino acid homology per residue (AAH/R)) (mean score: MBC/C < 1.25, AAH/R > 5.50; random sequences: MBC/C = 1.45, AAH/R = 4.46). Similarly, the predicted secondary structure of the repressor exhibits excellent agreement with the known secondary structures of the sugar-binding proteins. Using this primary sequence alignment, the tertiary structure of the core domain of the lac repressor has been modeled based on the known structures of the sugar-binding proteins as templates. While the structure deduced for the repressor is hypothetical, the model generated allows a comparison between the predicted tertiary arrangement and the wealth of genetic and chemical data elucidated for the repressor. Important residues involved in operator and sugar binding and in protein assembly have been identified using genetic methods, and placement of these residues in the model is consistent with their known function. This approach, therefore, provides a means to visualize the core domain of the lac repressor that allows interpretation of genetic and chemical data for specific residues and rational design of future experiments. | |||
Model of lactose repressor core based on alignment with sugar-binding proteins is concordant with genetic and chemical data.,Nichols JC, Vyas NK, Quiocho FA, Matthews KS J Biol Chem. 1993 Aug 15;268(23):17602-12. PMID:8349639<ref>PMID:8349639</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ltp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: Matthews, K S]] | [[Category: Matthews, K S]] | ||
[[Category: Nichols, J C]] | [[Category: Nichols, J C]] | ||
[[Category: Quiocho, F A]] | [[Category: Quiocho, F A]] | ||
[[Category: Vyas, N K]] | [[Category: Vyas, N K]] | ||
Latest revision as of 09:49, 18 August 2021
 |
MODEL OF LACTOSE REPRESSOR CORE BASED ON ALIGNMENT WITH SUGAR BINDING PROTEINS IS CONCORDANT WITH GENETIC AND CHEMICAL DATAMODEL OF LACTOSE REPRESSOR CORE BASED ON ALIGNMENT WITH SUGAR BINDING PROTEINS IS CONCORDANT WITH GENETIC AND CHEMICAL DATA
Structural highlights
Publication Abstract from PubMedUsing primary sequence similarity to arabinose-binding protein, D-glucose/D-galactose-binding protein, and ribose-binding protein (Vyas, N. K., Vyas, M. N., and Quiocho, F. A. (1991) J. Biol. Chem. 266, 5226-5237; Mowbray, S. L., and Cole, L. B. (1992) J. Mol. Biol. 225, 155-175), the core domain (residues 62-323) of the bacterial regulatory protein lac repressor has been aligned to these sugar-binding proteins of known structure. Although the sequence identity is not striking, there is strong overall homology based on two separate matrix scoring systems (minimum base change per codon (MBC/C) and amino acid homology per residue (AAH/R)) (mean score: MBC/C < 1.25, AAH/R > 5.50; random sequences: MBC/C = 1.45, AAH/R = 4.46). Similarly, the predicted secondary structure of the repressor exhibits excellent agreement with the known secondary structures of the sugar-binding proteins. Using this primary sequence alignment, the tertiary structure of the core domain of the lac repressor has been modeled based on the known structures of the sugar-binding proteins as templates. While the structure deduced for the repressor is hypothetical, the model generated allows a comparison between the predicted tertiary arrangement and the wealth of genetic and chemical data elucidated for the repressor. Important residues involved in operator and sugar binding and in protein assembly have been identified using genetic methods, and placement of these residues in the model is consistent with their known function. This approach, therefore, provides a means to visualize the core domain of the lac repressor that allows interpretation of genetic and chemical data for specific residues and rational design of future experiments. Model of lactose repressor core based on alignment with sugar-binding proteins is concordant with genetic and chemical data.,Nichols JC, Vyas NK, Quiocho FA, Matthews KS J Biol Chem. 1993 Aug 15;268(23):17602-12. PMID:8349639[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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