2a89: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2a89.png|left|200px]]
-{{STRUCTURE_2a89|  PDB=2a89  |  SCENE=  }}
+==Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme==
+<StructureSection load='2a89' size='340' side='right'caption='[[2a89]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[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]
+== 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/a8/2a89_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2a89 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme===
+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>
-{{ABSTRACT_PUBMED_16300392}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2a89" style="background-color:#fffaf0;"></div>
-[[2a89]] is a 2 chain structure with 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].
 ==See Also==
 *[[Sarcosine oxidase|Sarcosine oxidase]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:016300392</ref><ref group="xtra">PMID:010368302</ref><references group="xtra"/>
+__TOC__
-[[Category: Bacillus sp.]]
+</StructureSection>
-[[Category: Sarcosine oxidase]]
+[[Category: Bacillus sp. B-0618]]
-[[Category: Chen, Z W.]]
+[[Category: Large Structures]]
-[[Category: Jorns, M S.]]
+[[Category: Chen Z-W]]
-[[Category: Martinovic, S.]]
+[[Category: Jorns MS]]
-[[Category: Mathews, F S.]]
+[[Category: Martinovic S]]
-[[Category: Zhao, G.]]
+[[Category: Mathews FS]]
-[[Category: Flavoprotein]]
+[[Category: Zhao G]]
-[[Category: Oxidase]]
-[[Category: Oxidoreductase]]