3ad7: Difference between revisions
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==Heterotetrameric Sarcosine Oxidase from Corynebacterium sp. U-96 in complex with methylthio acetate== | |||
<StructureSection load='3ad7' size='340' side='right' caption='[[3ad7]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ad7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_sp._u-96 Corynebacterium sp. u-96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AD7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MTG:[METHYLTHIO]ACETATE'>MTG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x31|1x31]], [[1vrq|1vrq]], [[3ad8|3ad8]], [[3ad9|3ad9]], [[3ada|3ada]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">soxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31944 Corynebacterium sp. U-96]), soxB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31944 Corynebacterium sp. U-96]), soxG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31944 Corynebacterium sp. U-96]), soxD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31944 Corynebacterium sp. U-96])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sarcosine_oxidase Sarcosine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.1 1.5.3.1] </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=3ad7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ad7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ad7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ad7 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/ad/3ad7_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 == | |||
We characterized the crystal structures of heterotetrameric sarcosine oxidase (SO) from Corynebacterium sp. U-96 complexed with methylthioacetate (MTA), pyrrole 2-carboxylate (PCA), and sulfite, and of sarcosine-reduced SO. SO comprises alpha, beta, gamma , and delta subunits; FAD and FMN cofactors; and a large internal cavity. MTA and PCA are sandwiched between the re-face of the FAD isoalloxazine ring and the beta subunit C-terminal residues. Reduction of flavin cofactors shifts the beta subunit Ala1 toward the alpha subunit Met55, forming a surface cavity at the oxygen-channel vestibule and rendering the beta subunit C-terminal residues mobile. We identified three channels connecting the cavity and the enzyme surface. Two of them exist in the intersubunit space between alpha and beta subunits, and the substrate sarcosine seems to enter the active site through either of these channels and reaches the re-side of the FAD isoalloxazine ring by traversing the mobile beta subunit C-terminal residues. The third channel goes through the alpha subunit and has a folinic acid-binding site, where the iminium intermediate is converted to Gly and either formaldehyde or, 5,10-methylenetetrahydrofolate. Oxygen molecules are probably located on the surface cavity and diffuse to the FMN isoalloxazine ring; the H(2)O(2) formed exits via the oxygen channel. | |||
Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96.,Moriguchi T, Ida K, Hikima T, Ueno G, Yamamoto M, Suzuki H J Biochem. 2010 Aug 18. PMID:20675294<ref>PMID:20675294</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Sarcosine oxidase|Sarcosine oxidase]] | *[[Sarcosine oxidase|Sarcosine oxidase]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Corynebacterium sp. u-96]] | [[Category: Corynebacterium sp. u-96]] | ||
[[Category: Sarcosine oxidase]] | [[Category: Sarcosine oxidase]] | ||
[[Category: Ida, K | [[Category: Ida, K]] | ||
[[Category: Moriguchi, T | [[Category: Moriguchi, T]] | ||
[[Category: Suzuki, H | [[Category: Suzuki, H]] | ||
[[Category: Ligand complex]] | [[Category: Ligand complex]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||