2bra: Difference between revisions

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-[[Image:2bra.png|left|200px]]
-{{STRUCTURE_2bra|  PDB=2bra  |  SCENE=  }}
+==Structure of N-Terminal FAD Binding motif of mouse MICAL==
+<StructureSection load='2bra' size='340' side='right'caption='[[2bra]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bra]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BRA 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]] 2&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=2bra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bra OCA], [https://pdbe.org/2bra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bra RCSB], [https://www.ebi.ac.uk/pdbsum/2bra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bra ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MICA1_MOUSE MICA1_MOUSE] Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization. Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments (By similarity). Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4.
+== 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/br/2bra_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/main_output.php?pdb_ID=2bra ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+During development, neurons are guided to their targets by short- and long-range attractive and repulsive cues. MICAL, a large multidomain protein, is required for the combined action of semaphorins and plexins in axon guidance. Here, we present the structure of the N-terminal region of MICAL (MICAL(fd)) determined by x-ray diffraction to 2.0 A resolution. The structure shows that MICAL(fd) is an FAD-containing module structurally similar to aromatic hydroxylases and amine oxidases. In addition, we present biochemical data that show that MICAL(fd) is a flavoenzyme that in the presence of NADPH reduces molecular oxygen to H(2)O(2) (K(m,NAPDH) = 222 microM; k(cat) = 77 sec(-1)), a molecule with known signaling properties. We propose that the H(2)O(2) produced by this reaction may be one of the signaling molecules involved in axon guidance by MICAL.
-===STRUCTURE OF N-TERMINAL FAD BINDING MOTIF OF MOUSE MICAL===
+Structure and activity of the axon guidance protein MICAL.,Nadella M, Bianchet MA, Gabelli SB, Barrila J, Amzel LM Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16830-5. Epub 2005 Nov 7. PMID:16275926<ref>PMID:16275926</ref>
-{{ABSTRACT_PUBMED_16275926}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2bra" style="background-color:#fffaf0;"></div>
-[[2bra]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRA OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:016275926</ref><references group="xtra"/>
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Amzel, L M.]]
+[[Category: Amzel LM]]
-[[Category: Bianchet, M A.]]
+[[Category: Bianchet MA]]
-[[Category: Gabelli, S B.]]
+[[Category: Gabelli SB]]
-[[Category: Nadella, M.]]
+[[Category: Nadella M]]
-[[Category: Axon guidance]]
-[[Category: Cytoskeleton]]
-[[Category: Fad]]
-[[Category: Flavoprotein]]
-[[Category: Lim domain]]
-[[Category: Metal-binding]]
-[[Category: Plexin]]
-[[Category: Redox]]
-[[Category: Transport]]
-[[Category: Vesicle transport]]