This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6cww
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<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> | ||
| + | |||
| + | 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
| |||||||||||
