2ibn: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "2ibn" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image: | ==Crystal structure of Human myo-Inositol Oxygenase (MIOX)== | ||
<StructureSection load='2ibn' size='340' side='right' caption='[[2ibn]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ibn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IBN FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=I1N:(2S,3R,4R,5S,6S)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXANONE'>I1N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol_oxygenase Inositol oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.99.1 1.13.99.1] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ibn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ibn RCSB], [http://www.ebi.ac.uk/pdbsum/2ibn PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/2ibn_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Altered inositol metabolism is implicated in a number of diabetic complications. The first committed step in mammalian inositol catabolism is performed by myo-inositol oxygenase (MIOX), which catalyzes a unique four-electron dioxygen-dependent ring cleavage of myo-inositol to D-glucuronate. Here, we present the crystal structure of human MIOX in complex with myo-inosose-1 bound in a terminal mode to the MIOX diiron cluster site. Furthermore, from biochemical and biophysical results from N-terminal deletion mutagenesis we show that the N terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. EPR spectroscopy of the unliganded enzyme displays a two-component spectrum that we can relate to an open and a closed active site conformation. Furthermore, based on site-directed mutagenesis in combination with biochemical and biophysical data, we propose a novel role for Lys(127) in governing access to the diiron cluster. | |||
Structural and biophysical characterization of human myo-inositol oxygenase.,Thorsell AG, Persson C, Voevodskaya N, Busam RD, Hammarstrom M, Graslund S, Graslund A, Hallberg BM J Biol Chem. 2008 May 30;283(22):15209-16. Epub 2008 Mar 24. PMID:18364358<ref>PMID:18364358</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Inositol oxygenase]] | [[Category: Inositol oxygenase]] | ||
Revision as of 10:17, 30 September 2014
Crystal structure of Human myo-Inositol Oxygenase (MIOX)
| ||||||||||||
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Homo sapiens
- Inositol oxygenase
- Arrowsmith, C.
- Berg, S Van Den.
- Berglund, H.
- Busam, R D.
- Collins, R.
- Edwards, A.
- Ehn, M.
- Flodin, S.
- Flores, A.
- Graslund, S.
- Hallberg, B M.
- Hammarstrom, M.
- Hogbom, M.
- Holmberg-Schiavone, L.
- Johansson, I.
- Karlberg, T.
- Kotenyova, T.
- Nilsson-Ehle, P.
- Nordlund, P.
- Nyman, T.
- Ogg, D.
- Persson, C.
- SGC, Structural Genomics Consortium.
- Sagemark, J.
- Stenmark, P.
- Sundstrom, M.
- Thorsell, A G.
- Uppenberg, J.
- Weigelt, J.
- Diiron
- Inositol
- Oxidoreductase
- Reductase
- Sgc
- Structural genomic
- Structural genomics consortium
