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1e2b

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Revision as of 18:38, 10 March 2021

NMR STRUCTURE OF THE C10S MUTANT OF ENZYME IIB CELLOBIOSE OF THE PHOSPHOENOL-PYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI, 17 STRUCTURES

Structural highlights

1e2b is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PTQB_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 N,N'-diacetylchitobiose transport.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The assignment of the side-chain NMR resonances and the determination of the three-dimensional solution structure of the C10S mutant of enzyme IIBcellobiose (IIBcel) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli are presented. The side-chain resonances were assigned nearly completely using a variety of mostly heteronuclear NMR experiments, including HCCH-TOCSY, HCCH-COSY, and COCCH-TOCSY experiments as well as CBCACOHA, CBCA(CO)NH, and HBHA(CBCA)(CO)NH experiments. In order to obtain the three-dimensional structure, NOE data were collected from 15N-NOESY-HSQC, 13C-HSQC-NOESY, and 2D NOE experiments. The distance restraints derived from these NOE data were used in distance geometry calculations followed by molecular dynamics and simulated annealing protocols. In an iterative procedure, additional NOE assignments were derived from the calculated structures and new structures were calculated. The final set of structures, calculated with approximately 2000 unambiguous and ambiguous distance restraints, has an rms deviation of 1.1 A on C alpha atoms. IIBcel consists of a four stranded parallel beta-sheet, in the order 2134. The sheet is flanked with two and three alpha-helices on either side. Residue 10, a cysteine in the wild-type enzyme, which is phosphorylated during the catalytic cycle, is located at the end of the first beta-strand. A loop that is proposed to be involved in the binding of the phosphoryl-group follows the cysteine. The loop appears to be disordered in the unphosphorylated state.

The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.,Ab E, Schuurman-Wolters G, Reizer J, Saier MH, Dijkstra K, Scheek RM, Robillard GT Protein Sci. 1997 Feb;6(2):304-14. PMID:9041631^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Keyhani NO, Wang LX, Lee YC, Roseman S. The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J Biol Chem. 2000 Oct 20;275(42):33084-90. PMID:10913117 doi:http://dx.doi.org/10.1074/jbc.M001043200
↑ Ab E, Schuurman-Wolters G, Reizer J, Saier MH, Dijkstra K, Scheek RM, Robillard GT. The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Sci. 1997 Feb;6(2):304-14. PMID:9041631

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e2b"

@@ Line 3: / Line 3: @@
 <StructureSection load='1e2b' size='340' side='right'caption='[[1e2b]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e2b]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e2b]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E2B FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span></td></tr>
+</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>
-<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=1e2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2b OCA], [http://pdbe.org/1e2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2b RCSB], [http://www.ebi.ac.uk/pdbsum/1e2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2b ProSAT]</span></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=1e2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2b OCA], [https://pdbe.org/1e2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e2b RCSB], [https://www.ebi.ac.uk/pdbsum/1e2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTQB_ECOLI PTQB_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 N,N'-diacetylchitobiose transport.<ref>PMID:10913117</ref>
+[[https://www.uniprot.org/uniprot/PTQB_ECOLI PTQB_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 N,N'-diacetylchitobiose transport.<ref>PMID:10913117</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1e2b

From Proteopedia

Revision as of 18:38, 10 March 2021

NMR STRUCTURE OF THE C10S MUTANT OF ENZYME IIB CELLOBIOSE OF THE PHOSPHOENOL-PYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI, 17 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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