6cww
From Proteopedia
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<StructureSection load='6cww' size='340' side='right' caption='[[6cww]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='6cww' size='340' side='right' caption='[[6cww]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6cww]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CWW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cww]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-225 Atcc baa-225]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CWW FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=211:2,2,2-NITRILOTRIETHANOL'>211</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=211:2,2,2-NITRILOTRIETHANOL'>211</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CF:4-CYANO-L-PHENYLALANINE'>4CF</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CF:4-CYANO-L-PHENYLALANINE'>4CF</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XD49_1849 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=911092 ATCC BAA-225])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cww OCA], [http://pdbe.org/6cww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cww RCSB], [http://www.ebi.ac.uk/pdbsum/6cww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cww ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cww OCA], [http://pdbe.org/6cww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cww RCSB], [http://www.ebi.ac.uk/pdbsum/6cww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cww ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The vibrational reporter unnatural amino acid (UAA) 4-cyano-l-phenylalanine (pCNF) was genetically incorporated individually at three sites (5, 36, and 78) in the heme protein Caldanaerobacter subterraneus H-NOX to probe local hydration environments. The UAA pCNF was incorporated site-specifically using an engineered, orthogonal tRNA synthetase in E. coli. The ability of all of the pCNF-containing H-NOX proteins to form the ferrous CO, NO, or O2 ligated and unligated states was confirmed with UV-Vis spectroscopy. The solvation state at each site of the three sites of pCNF incorporation was assessed using temperature-dependent infrared spectroscopy. Specifically, the frequency-temperature line slope (FTLS) method was utilized to show that the nitrile group at site 36 was fully solvated and the nitrile group at site 78 was de-solvated (buried) in the heme pocket. The nitrile group at site 5 was found to be partially solvated suggesting that the nitrile group was involved in moderate strength hydrogen bonds. These results were confirmed by the determination of the X-ray crystal structure of the H-NOX protein construct containing pCNF at site 5. | ||
| + | |||
| + | Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine.,Kearney C, Olenginski LT, Hirn TD, Fowler GD, Tariq D, Brewer SH, Phillips-Piro CM RSC Adv. 2018 Apr 9;8(24):13503-13512. doi: 10.1039/c8ra02000k. Epub 2018 Apr 10. PMID:29780583<ref>PMID:29780583</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6cww" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc baa-225]] | ||
[[Category: Brewer, S H]] | [[Category: Brewer, S H]] | ||
[[Category: Fowler, G D]] | [[Category: Fowler, G D]] | ||
Revision as of 06:21, 6 June 2018
Cs H-NOX mutant with unnatural amino acid 4-cyano-L-phenylalanine at site 5
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