View source for 5woy


==NMR solution structure of Enzyme I (nEIt) protein using two 4D-spectra==
<StructureSection load='5woy' size='340' side='right'caption='[[5woy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5woy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WOY 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=5woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5woy OCA], [https://pdbe.org/5woy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5woy RCSB], [https://www.ebi.ac.uk/pdbsum/5woy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5woy ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/Q8R7R4_CALS4 Q8R7R4_CALS4] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).[PIRNR:PIRNR000732]
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== Publication Abstract from PubMed ==
Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.

Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.,Evangelidis T, Nerli S, Novacek J, Brereton AE, Karplus PA, Dotas RR, Venditti V, Sgourakis NG, Tripsianes K Nat Commun. 2018 Jan 26;9(1):384. doi: 10.1038/s41467-017-02592-z. PMID:29374165<ref>PMID:29374165</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]]
[[Category: Large Structures]]
[[Category: Evangelidis T]]
[[Category: Nerli S]]
[[Category: Sgourakis NG]]
[[Category: Tripsianes K]]