1f3g

<table><tr><td colspan='2'>[[1f3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3G 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=1f3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3g OCA], [https://pdbe.org/1f3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3g RCSB], [https://www.ebi.ac.uk/pdbsum/1f3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3g ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/PTGA_ECOLI PTGA_ECOLI]] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.

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== Publication Abstract from PubMed ==

The crystal structure of a proteolytically modified form of the Escherichia coli phosphocarrier and signal transducing protein IIIglc has been determined by multiple isomorphous and molecular replacement. The model has been refined to an R-factor of 0.166 for data between 6- and 2.1-A resolution with an rms deviation of 0.020 A from ideal bond lengths and 3.2 degrees from ideal bond angles. The molecule is a beta-sheet sandwich, with six antiparallel strands on either side. Several short distorted helices line the periphery of the active site, which is a shallow extremely hydrophobic depression approximately 18 A in diameter near the center of one face. The side chains of the active site histidine residues 75 and 90 face each other at the center of the depression, with the N3 positions exposed to solvent, separated by 3.3 A in an excellent position to form adducts with phosphate. Chloroplatinate forms a divalent adduct with both histidyl side chains, suggesting that the phosphodonor reaction might proceed through a similar transition state. The hydrophobic patch forms the primary crystal contact, suggesting a mode of association of IIIglc with other components of the phosphoenolpyruvate-dependent phosphotransferase system.

Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc.,Worthylake D, Meadow ND, Roseman S, Liao DI, Herzberg O, Remington SJ Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10382-6. PMID:1961703<ref>PMID:1961703</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Herzberg, O]]

[[Category: Liao, D I]]

[[Category: Meadow, N]]

[[Category: Remington, S J]]

[[Category: Roseman, S]]

[[Category: Worthylake, D]]

[[Category: Phosphotransferase]]