4fc1
From Proteopedia
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| - | [[Image:4fc1.jpg|left|200px]] | ||
| - | + | ==Ultra-high resolution neutron structure of crambin at room-temperature== | |
| + | <StructureSection load='4fc1' size='340' side='right'caption='[[4fc1]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4fc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FC1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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=4fc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fc1 OCA], [https://pdbe.org/4fc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fc1 RCSB], [https://www.ebi.ac.uk/pdbsum/4fc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fc1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 1.1 A, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out of 315, or 94.9%, of the hydrogen atom positions in the protein have been experimentally derived and resolved through nuclear density maps. A number of unconventional interactions are clearly defined, including a potential O horizontal line H...pi interaction between a water molecule and the aromatic ring of residue Y44, as well as a number of potential C horizontal line H...O hydrogen bonds. Hydrogen bonding networks that are ambiguous in the 0.85 A ultrahigh resolution X-ray structure can be resolved by accurate orientation of water molecules. Furthermore, the high resolution of the reported structure has allowed for the anisotropic description of 36 deuterium atoms in the protein. The visibility of hydrogen and deuterium atoms in the nuclear density maps is discussed in relation to the resolution of the neutron data. | ||
| - | + | Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography.,Chen JC, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY Proc Natl Acad Sci U S A. 2012 Sep 4. PMID:22949690<ref>PMID:22949690</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 4fc1" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Crambe hispanica subsp. abyssinica]] | [[Category: Crambe hispanica subsp. abyssinica]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Chen JC-H]] | |
| - | [[Category: H | + | [[Category: Kovalevsky AY]] |
| - | [[Category: | + | |
| - | + | ||
Current revision
Ultra-high resolution neutron structure of crambin at room-temperature
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