5t1n

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==Solution-state NMR structural ensemble of NPr (1-85) refined with RDCs and PCS==
==Solution-state NMR structural ensemble of NPr (1-85) refined with RDCs and PCS==
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<StructureSection load='5t1n' size='340' side='right'caption='[[5t1n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5t1n' size='340' side='right'caption='[[5t1n]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t1n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T1N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t1n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T1N FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptsO, Z4569, ECs4085 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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=5t1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t1n OCA], [http://pdbe.org/5t1n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t1n RCSB], [http://www.ebi.ac.uk/pdbsum/5t1n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t1n ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t1n OCA], [https://pdbe.org/5t1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t1n RCSB], [https://www.ebi.ac.uk/pdbsum/5t1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t1n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PTSO_ECO57 PTSO_ECO57]] Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to EIIA-Ntr. Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins (By similarity).
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[https://www.uniprot.org/uniprot/PTSO_ECOLI PTSO_ECOLI] Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to EIIA-Ntr. Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Paralogous enzymes arise from gene duplication events that confer a novel function, although it is unclear how cross-reaction between the original and duplicate protein interaction network is minimized. We investigated HPr:EIsugar and NPr:EINtr, the initial complexes of paralogous phosphorylation cascades involved in sugar import and nitrogen regulation in bacteria, respectively. Although the HPr:EIsugar interaction has been well characterized, involving multiple complexes and transient interactions, the exact nature of the NPr:EINtr complex was unknown. We set out to identify the key features of the interaction by performing binding assays and elucidating the structure of NPr in complex with the phosphorylation domain of EINtr (EINNtr), using a hybrid approach involving X-ray, homology, and sparse nuclear magnetic resonance. We found that the overall fold and active-site structure of the two complexes are conserved in order to maintain productive phosphorylation, however, the interface surface potential differs between the two complexes, which prevents cross-reaction.
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Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.,Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N Structure. 2016 Dec 6;24(12):2127-2137. doi: 10.1016/j.str.2016.10.007. Epub 2016, Nov 10. PMID:27839951<ref>PMID:27839951</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5t1n" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eco57]]
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[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peterkofsky, A]]
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[[Category: Peterkofsky A]]
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[[Category: Strickland, M]]
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[[Category: Strickland M]]
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[[Category: Tjandra, N]]
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[[Category: Tjandra N]]
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[[Category: Wang, G]]
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[[Category: Wang G]]
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[[Category: Bacterial]]
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[[Category: Hpr-like]]
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[[Category: Phosphotransfer]]
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[[Category: Ptsntr]]
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[[Category: Transferase]]
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Current revision

Solution-state NMR structural ensemble of NPr (1-85) refined with RDCs and PCS

PDB ID 5t1n

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