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| | <StructureSection load='5lgx' size='340' side='right'caption='[[5lgx]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='5lgx' size='340' side='right'caption='[[5lgx]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lgx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LGX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lgx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LGX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">onr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 "Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgx OCA], [http://pdbe.org/5lgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lgx RCSB], [http://www.ebi.ac.uk/pdbsum/5lgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgx 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=5lgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgx OCA], [https://pdbe.org/5lgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lgx RCSB], [https://www.ebi.ac.uk/pdbsum/5lgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P71278_ENTCL P71278_ENTCL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Enterobacter cloacae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kwon, H]] | + | [[Category: Kwon H]] |
| - | [[Category: Moody, P C.E]] | + | [[Category: Moody PCE]] |
| - | [[Category: Smith, O M]] | + | [[Category: Smith OM]] |
| - | [[Category: Fmn]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Petn reductase]]
| + | |
| - | [[Category: Petnr]]
| + | |
| Structural highlights
Function
P71278_ENTCL
Publication Abstract from PubMed
X-ray protein crystallography has, through the determination of the three-dimensional structures of enzymes and their complexes, been essential to the understanding of biological chemistry. However, as X-rays are scattered by electrons, the technique has difficulty locating the presence and position of H atoms (and cannot locate H+ ions), knowledge of which is often crucially important for the understanding of enzyme mechanism. Furthermore, X-ray irradiation, through photoelectronic effects, will perturb the redox state in the crystal. By using single-crystal spectrophotometry, reactions taking place in the crystal can be monitored, either to trap intermediates or follow photoreduction during X-ray data collection. By using neutron crystallography, the positions of H atoms can be located, as it is the nuclei rather than the electrons that scatter neutrons, and the scattering length is not determined by the atomic number. Combining the two techniques allows much greater insight into both reaction mechanism and X-ray-induced photoreduction.
Combining X-ray and neutron crystallography with spectroscopy.,Kwon H, Smith O, Raven EL, Moody PC Acta Crystallogr D Struct Biol. 2017 Feb 1;73(Pt 2):141-147. doi:, 10.1107/S2059798316016314. Epub 2017 Feb 1. PMID:28177310[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kwon H, Smith O, Raven EL, Moody PC. Combining X-ray and neutron crystallography with spectroscopy. Acta Crystallogr D Struct Biol. 2017 Feb 1;73(Pt 2):141-147. doi:, 10.1107/S2059798316016314. Epub 2017 Feb 1. PMID:28177310 doi:http://dx.doi.org/10.1107/S2059798316016314
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