2bra

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2bra" [edit=sysop:move=sysop])
Current revision (09:18, 9 May 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[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: 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]]
+

Current revision

Structure of N-Terminal FAD Binding motif of mouse MICAL

PDB ID 2bra

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bra"
Personal tools