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2a89

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[[Image:2a89.gif|left|200px]]
 
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==Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme==
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The line below this paragraph, containing "STRUCTURE_2a89", creates the "Structure Box" on the page.
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<StructureSection load='2a89' size='340' side='right'caption='[[2a89]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2a89]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._B-0618 Bacillus sp. B-0618]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A89 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FCG:(N5,C4A)-(ALPHA-HYDROXY-PROPANO)-3,4,4A,5-TETRAHYDRO-FLAVIN-ADENINE+DINUCLEOTIDE'>FCG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_2a89| PDB=2a89 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a89 OCA], [https://pdbe.org/2a89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a89 RCSB], [https://www.ebi.ac.uk/pdbsum/2a89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a89 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MSOX_BACB0 MSOX_BACB0] Catalyzes the oxidative demethylation of sarcosine. Can also oxidize other secondary amino acids such as N-methyl-L-alanine.[HAMAP-Rule:MF_00516]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/2a89_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2a89 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Monomeric sarcosine oxidase (MSOX) is a flavoprotein that contains covalently bound FAD [8a-(S-cysteinyl)FAD] and catalyzes the oxidation of sarcosine (N-methylglycine) and other secondary amino acids, such as l-proline. Our previous studies showed that N-(cyclopropyl)glycine (CPG) acts as a mechanism-based inactivator of MSOX [Zhao, G., et al. (2000) Biochemistry 39, 14341-14347]. The reaction results in the formation of a modified reduced flavin that can be further reduced and stabilized by treatment with sodium borohydride. The borohydride-reduced CPG-modified enzyme exhibits a mass increase of 63 +/- 2 Da as compared with native MSOX. The crystal structure of the modified enzyme, solved at 1.85 A resolution, shows that FAD is the only site of modification. The modified FAD contains a fused five-membered ring, linking the C(4a) and N(5) atoms of the flavin ring, with an additional oxygen atom bound to the carbon atom attached to N(5) and a tetrahedral carbon atom at flavin C(4) with a hydroxyl group attached to C(4). On the basis of the crystal structure of the borohydride-stabilized adduct, we conclude that the labile CPG-modified flavin is a 4a,5-dihydroflavin derivative with a substituent derived from the cleavage of the cyclopropyl ring in CPG. The results are consistent with CPG-mediated inactivation in a reaction initiated by single electron transfer from the amine function in CPG to FAD in MSOX, followed by collapse of the radical pair to yield a covalently modified 4a,5-dihydroflavin.
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'''Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme'''
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Structure of the sodium borohydride-reduced N-(cyclopropyl)glycine adduct of the flavoenzyme monomeric sarcosine oxidase.,Chen ZW, Zhao G, Martinovic S, Jorns MS, Mathews FS Biochemistry. 2005 Nov 29;44(47):15444-50. PMID:16300392<ref>PMID:16300392</ref>
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==Overview==
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Monomeric sarcosine oxidase (MSOX) is a flavoprotein that contains covalently bound FAD [8a-(S-cysteinyl)FAD] and catalyzes the oxidation of sarcosine (N-methylglycine) and other secondary amino acids, such as l-proline. Our previous studies showed that N-(cyclopropyl)glycine (CPG) acts as a mechanism-based inactivator of MSOX [Zhao, G., et al. (2000) Biochemistry 39, 14341-14347]. The reaction results in the formation of a modified reduced flavin that can be further reduced and stabilized by treatment with sodium borohydride. The borohydride-reduced CPG-modified enzyme exhibits a mass increase of 63 +/- 2 Da as compared with native MSOX. The crystal structure of the modified enzyme, solved at 1.85 A resolution, shows that FAD is the only site of modification. The modified FAD contains a fused five-membered ring, linking the C(4a) and N(5) atoms of the flavin ring, with an additional oxygen atom bound to the carbon atom attached to N(5) and a tetrahedral carbon atom at flavin C(4) with a hydroxyl group attached to C(4). On the basis of the crystal structure of the borohydride-stabilized adduct, we conclude that the labile CPG-modified flavin is a 4a,5-dihydroflavin derivative with a substituent derived from the cleavage of the cyclopropyl ring in CPG. The results are consistent with CPG-mediated inactivation in a reaction initiated by single electron transfer from the amine function in CPG to FAD in MSOX, followed by collapse of the radical pair to yield a covalently modified 4a,5-dihydroflavin.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2A89 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A89 OCA].
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</div>
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<div class="pdbe-citations 2a89" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structure of the sodium borohydride-reduced N-(cyclopropyl)glycine adduct of the flavoenzyme monomeric sarcosine oxidase., Chen ZW, Zhao G, Martinovic S, Jorns MS, Mathews FS, Biochemistry. 2005 Nov 29;44(47):15444-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16300392 16300392]
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*[[Sarcosine oxidase|Sarcosine oxidase]]
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[[Category: Bacillus sp.]]
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== References ==
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[[Category: Sarcosine oxidase]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Chen, Z W.]]
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</StructureSection>
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[[Category: Jorns, M S.]]
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[[Category: Bacillus sp. B-0618]]
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[[Category: Martinovic, S.]]
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[[Category: Large Structures]]
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[[Category: Mathews, F S.]]
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[[Category: Chen Z-W]]
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[[Category: Zhao, G.]]
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[[Category: Jorns MS]]
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[[Category: Flavoprotein]]
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[[Category: Martinovic S]]
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[[Category: Oxidase]]
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[[Category: Mathews FS]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:44:07 2008''
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[[Category: Zhao G]]

Current revision

Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme

PDB ID 2a89

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