4pyt: Difference between revisions
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<StructureSection load='4pyt' size='340' side='right'caption='[[4pyt]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='4pyt' size='340' side='right'caption='[[4pyt]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pyt]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4pyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PYT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.853Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pyt OCA], [https://pdbe.org/4pyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pyt RCSB], [https://www.ebi.ac.uk/pdbsum/4pyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pyt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MURB_BACLD MURB_BACLD] Cell wall formation.[HAMAP-Rule:MF_00037] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Unidentified]] | ||
[[Category: Auldridge M]] | |||
[[Category: Auldridge | [[Category: Bingman C]] | ||
[[Category: Bingman | [[Category: Cao H]] | ||
[[Category: Cao | [[Category: Franz L]] | ||
[[Category: Franz | [[Category: Mead D]] | ||
[[Category: Mead | [[Category: Phillips Jr GN]] | ||
[[Category: Phillips | [[Category: Sen S]] | ||
[[Category: Sen | [[Category: Steinmetz E]] | ||
[[Category: Steinmetz | |||
Latest revision as of 12:49, 22 May 2024
Crystal structure of a MurB family EP-UDP-N-acetylglucosamine reductaseCrystal structure of a MurB family EP-UDP-N-acetylglucosamine reductase
Structural highlights
FunctionMURB_BACLD Cell wall formation.[HAMAP-Rule:MF_00037] Publication Abstract from PubMedWe report on the discovery, isolation, and use of a novel yellow fluorescent protein. Lucigen Yellow (LucY) binds one FAD molecule within its core, thus shielding it from water and maintaining its structure so that fluorescence is 10-fold higher than freely soluble FAD. LucY displays excitation and emission spectra characteristic of FAD, with 3 excitation peaks at 276 nm, 377 nm, and 460 nm and a single emission peak at 530 nm. These excitation and emission maxima provide the large Stokes shift beneficial to fluorescence experimentation. LucY belongs to the MurB family of UDP-N-acetylenolpyruvylglucosamine reductases. The high resolution crystal structure shows that in contrast to other structurally resolved MurB enzymes, LucY does not contain a potentially quenching aromatic residue near the FAD isoalloxazine ring, which may explain its increased fluorescence over related proteins. Using E. coli as a system in which to develop LucY as a reporter, we show that it is amenable to circular permutation and use as a reporter of protein-protein interaction. Fragmentation between its distinct domains renders LucY non-fluorescent, but fluorescence can be partially restored by fusion of the fragments to interacting protein domains. Thus, LucY may find application in Protein-fragment Complementation Assays for evaluating protein-protein interactions. LucY: A Versatile New Fluorescent Reporter Protein.,Auldridge ME, Cao H, Sen S, Franz LP, Bingman CA, Yennamalli RM, Phillips GN Jr, Mead D, Steinmetz EJ PLoS One. 2015 Apr 23;10(4):e0124272. doi: 10.1371/journal.pone.0124272., eCollection 2015. PMID:25906065[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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