1ax3

<StructureSection load='1ax3' size='340' side='right'caption='[[1ax3]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ax3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AX3 FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span></td></tr>

[[https://www.uniprot.org/uniprot/PTG3C_BACSU PTG3C_BACSU]] 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 high-resolution solution structure of the phosphocarrier protein IIAglc from Bacillus subtilis is determined using 3D and 4D heteronuclear NMR methods. B. subtilis IIAglc contains 162 amino acid residues and is one of the larger proteins for which high-resolution solution structure has been determined by NMR methods. The structures have been calculated from a total of 2,232 conformational constraints. Comparison with the X-ray crystal structure indicates that the overall fold is the same in solution and in crystalline environments, although some local structural differences are observed. These occur largely in turns and loops, and mostly correspond to regions with high-temperature factors in the crystal structure. The N-terminus of IIAglc is disordered in solution. The active site is located in a concave region of the protein surface. The histidine, which accepts the phosphoryl group (His 83), interacts with a neighboring histidine (His 68) and is surrounded by hydrophobic residues.

High-resolution solution structure of Bacillus subtilis IIAglc.,Chen Y, Case DA, Reizer J, Saier MH Jr, Wright PE Proteins. 1998 May 15;31(3):258-70. PMID:9593197<ref>PMID:9593197</ref>

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

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== References ==

<references/>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Case, D A]]

[[Category: Chen, Y]]

[[Category: Junior, M H.Saier]]

[[Category: Reizer, J]]

[[Category: Wright, P E]]

[[Category: Phosphorylation]]

[[Category: Transmembrane]]