1ihc: Difference between revisions

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-[[Image:1ihc.gif|left|200px]]
-<!--
+==X-ray Structure of Gephyrin N-terminal Domain==
-The line below this paragraph, containing "STRUCTURE_1ihc", creates the "Structure Box" on the page.
+<StructureSection load='1ihc' size='340' side='right'caption='[[1ihc]], [[Resolution|resolution]] 1.90&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'>[[1ihc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHC 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]] 1.9&#8491;</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=1ihc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihc OCA], [https://pdbe.org/1ihc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ihc RCSB], [https://www.ebi.ac.uk/pdbsum/1ihc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ihc ProSAT]</span></td></tr>
-{{STRUCTURE_1ihc|  PDB=1ihc  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GEPH_RAT GEPH_RAT] Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.<ref>PMID:8264797</ref> <ref>PMID:9990024</ref>
+== 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/ih/1ihc_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=1ihc ConSurf].
+<div style="clear:both"></div>
-'''X-ray Structure of Gephyrin N-terminal Domain'''
+==See Also==
+*[[Gephyrin|Gephyrin]]
+== References ==
-==Overview==
+<references/>
-Gephyrin is a ubiquitously expressed protein that, in the central nervous system, forms a submembraneous scaffold for anchoring inhibitory neurotransmitter receptors in the postsynaptic membrane. The N- and C-terminal domains of gephyrin are homologous to the Escherichia coli enzymes MogA and MoeA, respectively, both of which are involved in molybdenum cofactor biosynthesis. This enzymatic pathway is highly conserved from bacteria to mammals, as underlined by the ability of gephyrin to rescue molybdenum cofactor deficiencies in different organisms. Here we report the x-ray crystal structure of the N-terminal domain (amino acids 2-188) of rat gephyrin at 1.9-A resolution. Gephyrin-(2-188) forms trimers in solution, and a sequence motif thought to be involved in molybdopterin binding is highly conserved between gephyrin and the E. coli protein. The atomic structure of gephyrin-(2-188) resembles MogA, albeit with two major differences. The path of the C-terminal ends of gephyrin-(2-188) indicates that the central and C-terminal domains, absent in this structure, should follow a similar 3-fold arrangement as the N-terminal region. In addition, a central beta-hairpin loop found in MogA is lacking in gephyrin-(2-188). Despite these differences, both structures show a high degree of surface charge conservation, which is consistent with their common catalytic function.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-IHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHC OCA].
-==Reference==
-X-ray crystal structure of the trimeric N-terminal domain of gephyrin., Sola M, Kneussel M, Heck IS, Betz H, Weissenhorn W, J Biol Chem. 2001 Jul 6;276(27):25294-301. Epub 2001 Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11325967 11325967]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Betz H]]
-[[Category: Betz, H.]]
+[[Category: Heck IS]]
-[[Category: Heck, I S.]]
+[[Category: Kneussel M]]
-[[Category: Kneussel, M.]]
+[[Category: Sola M]]
-[[Category: Sola, M.]]
+[[Category: Weissenhorn W]]
-[[Category: Weissenhorn, W.]]
-[[Category: Alpha/beta]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:00:04 2008''