7lvc
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7lvc is ON HOLD Authors: Greisman, J.B., Dalton, K.M., Hekstra, D.R. Description: E. coli DHFR by Native Mn,P,S-SAD at Room Temperature [[Category:...) |
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- | '''Unreleased structure''' | ||
- | + | ==E. coli DHFR by Native Mn,P,S-SAD at Room Temperature== | |
+ | <StructureSection load='7lvc' size='340' side='right'caption='[[7lvc]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[7lvc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LVC FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=7lvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lvc OCA], [https://pdbe.org/7lvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lvc RCSB], [https://www.ebi.ac.uk/pdbsum/7lvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lvc ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[https://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature. | ||
- | + | Native SAD phasing at room temperature.,Greisman JB, Dalton KM, Sheehan CJ, Klureza MA, Kurinov I, Hekstra DR Acta Crystallogr D Struct Biol. 2022 Aug 1;78(Pt 8):986-996. doi:, 10.1107/S2059798322006799. Epub 2022 Jul 27. PMID:35916223<ref>PMID:35916223</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 7lvc" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | |
- | [[Category: | + | ==See Also== |
+ | *[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Escherichia coli K-12]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Dalton KM]] | ||
+ | [[Category: Greisman JB]] | ||
+ | [[Category: Hekstra DR]] |
Current revision
E. coli DHFR by Native Mn,P,S-SAD at Room Temperature
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