3zyx: Difference between revisions

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-[[Image:3zyx.jpg|left|200px]]
-<!--
+==Crystal structure of human monoamine oxidase B in complex with methylene blue and bearing the double mutation I199A-Y326A==
-The line below this paragraph, containing "STRUCTURE_3zyx", creates the "Structure Box" on the page.
+<StructureSection load='3zyx' size='340' side='right'caption='[[3zyx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3zyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYX FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MBT:3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM'>MBT</scene></td></tr>
-{{STRUCTURE_3zyx|  PDB=3zyx  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyx OCA], [https://pdbe.org/3zyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyx RCSB], [https://www.ebi.ac.uk/pdbsum/3zyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The major structural difference between human monoamine oxidases A (MAO A) and B (MAO B) is that MAO A has a monopartite substrate cavity of approximately 550 A(3) volume and MAO B contains a dipartite cavity structure with volumes of approximately 290 A(3) (entrance cavity) and approximately 400 A(3) (substrate cavity). Ile199 and Tyr326 side chains separate these two cavities in MAO B. To probe the function of these gating residues, Ile199Ala and Ile199Ala-Tyr326Ala mutant forms of MAO B were investigated. Structural data on the Ile199Ala MAO B mutant show no alterations in active site geometries compared with wild-type enzyme while the Ile199Ala-Tyr326Ala MAO B mutant exhibits alterations in residues 100-103 which are part of the loop gating the entrance to the active site. Both mutant enzymes exhibit catalytic properties with increased amine K(M) but unaltered k(cat) values. The altered K(M) values on mutation are attributed to the influence of the cavity structure in the binding and subsequent deprotonation of the amine substrate. Both mutant enzymes exhibit weaker binding affinities relative to wild-type enzyme for small reversible inhibitors. Ile199Ala MAO B exhibits an increase in binding affinity for reversible MAO B specific inhibitors which bridge both cavities. The Ile199Ala-Tyr326Ala double mutant exhibits inhibitor binding properties more similar to those of MAO A than to MAO B. These results demonstrate that the bipartite cavity structure in MAO B plays an important role in substrate and inhibitor recognition to distinguish its specificities from those of MAO A and provide insights into specific reversible inhibitor design for these membrane-bound enzymes. Database The atomic coordinates and structural factors of the structure of human MAO B Ile199Ala-Tyr326Ala double mutant have been deposited in the Protein Data Bank under the accession number 3zyx.
-===CRYSTAL STRUCTURE OF HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH METHYLENE BLUE AND BEARING THE DOUBLE MUTATION I199A-Y326A===
+The 'gating' residues Ile199 and Tyr326 in human monoamine oxidase B function in substrate and inhibitor recognition.,Milczek EM, Binda C, Rovida S, Mattevi A, Edmondson DE FEBS J. 2011 Dec;278(24):4860-9. doi: 10.1111/j.1742-4658.2011.08386.x., Epub 2011 Nov 3. PMID:21978362<ref>PMID:21978362</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3zyx" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21978362}}, adds the Publication Abstract to the page
+*[[Monoamine oxidase|Monoamine oxidase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21978362 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21978362}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[3zyx]] 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=3ZYX OCA].
-==Reference==
-<ref group="xtra">PMID:021978362</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Monoamine oxidase]]
+[[Category: Large Structures]]
-[[Category: Binda, C.]]
+[[Category: Binda C]]
-[[Category: Edmondson, D E.]]
+[[Category: Edmondson DE]]
-[[Category: Mattevi, A.]]
+[[Category: Mattevi A]]
-[[Category: Milczek, E M.]]
+[[Category: Milczek EM]]
-[[Category: Rovida, S.]]
+[[Category: Rovida S]]
-[[Category: Inhibitor]]
-[[Category: Oxidoreductase]]