2jz7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
<StructureSection load='2jz7' size='340' side='right' caption='[[2jz7]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2jz7' size='340' side='right' caption='[[2jz7]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jz7]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2jz7]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35089 Atcc 35089]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZ7 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2187 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2187 ATCC 35089])</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=2jz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jz7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jz7 RCSB], [http://www.ebi.ac.uk/pdbsum/2jz7 PDBsum]</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=2jz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jz7 OCA], [http://pdbe.org/2jz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jz7 RCSB], [http://www.ebi.ac.uk/pdbsum/2jz7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 14: | Line 14: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2jz7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 35089]] | ||
[[Category: Stadtman, T C]] | [[Category: Stadtman, T C]] | ||
[[Category: Suzuki, M]] | [[Category: Suzuki, M]] | ||
Revision as of 12:10, 10 September 2015
Solution NMR structure of selenium-binding protein from Methanococcus VannieliiSolution NMR structure of selenium-binding protein from Methanococcus Vannielii
Structural highlights
Publication Abstract from PubMedSelenium is an important nutrient. Lack of selenium will suppress expression of various enzymes, that will lead to cell abnormality and diseases. However, high concentrations of free selenium are toxic to the cell because it adversely affects numerous cell metabolism pathways. In Methanonoccus vannielii, selenium transport in the cell is established by the selenium binding protein, SeBP. SeBP sequesters selenium during transport, thus regulating the level of free selenium in the cell, and delivers it specifically to the selenophosphate synthase enzyme. In solution, SeBP is an oligomer of 8.8 kDa subunits. It is a symmetric pentamer. The solution structure of SeBP was determined by Nuclear Magnetic Resonance spectroscopy. Each subunit of SeBP is composed of an a-helix on top of a 4-stranded twisted ss-sheet. The stability of the five subunits stems mainly from hydrophobic interactions, and supplemented by hydrogen bonds interactions. The loop containing Cys59, which has been shown to be important for selenium binding, is flexible and adopts multiple conformations. However, the cysteine accessibility is restricted in the structure, reducing the possibility of binding of free selenium readily. Therefore a different selenium precursor or other factors might be needed to facilitate opening of this loop to expose Cys59 for selenium binding. Solution NMR structure of selenium-binding protein from methanococcus vannielii.,Suzuki M, Lee DY, Inyamah N, Stadtman TC, Tjandra N J Biol Chem. 2008 Jul 23. PMID:18650445[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||