1fma: Difference between revisions

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OCA

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-[[Image:1fma.gif|left|200px]]<br /><applet load="1fma" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fma, resolution 1.58&Aring;" />
-'''MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)'''<br />
-==Overview==
+==MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)==
-Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved, pathway present in eubacteria, archaea and eukaryotes, including humans., Genetic deficiencies of enzymes involved in Moco biosynthesis in humans, lead to a severe and usually fatal disease. Moco contains a tricyclic, pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene, group responsible for molybdenum ligation. The dithiolene group of MPT is, generated by MPT synthase, which consists of a large and small subunits., The 1.45 A resolution crystal structure of MPT synthase reveals a, heterotetrameric protein in which the C-terminus of each small subunit is, inserted into a large subunit to form the active site. In the activated, form of the enzyme this C-terminus is present as a thiocarboxylate. In the, structure of a covalent complex of MPT synthase, an isopeptide bond is, present between the C-terminus of the small subunit and a Lys side chain, in the large subunit. The strong structural similarity between the small, subunit of MPT synthase and ubiquitin provides evidence for the, evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin, dependent protein degradation pathway.
+<StructureSection load='1fma' size='340' side='right'caption='[[1fma]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1fma]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMA FirstGlance]. <br>
-FMA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FMA OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#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></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fma OCA], [https://pdbe.org/1fma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fma RCSB], [https://www.ebi.ac.uk/pdbsum/1fma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fma ProSAT]</span></td></tr>
-Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation., Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H, Nat Struct Biol. 2001 Jan;8(1):42-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11135669 11135669]
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MOAD_ECOLI MOAD_ECOLI] Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.<ref>PMID:17223713</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/fm/1fma_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=1fma ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Rajagolpalan, K.V.]]
+[[Category: Rajagolpalan KV]]
-[[Category: Rudolph, M.J.]]
+[[Category: Rudolph MJ]]
-[[Category: Schindelin, H.]]
+[[Category: Schindelin H]]
-[[Category: Wuebbens, M.M.]]
+[[Category: Wuebbens MM]]
-[[Category: CL]]
-[[Category: isopeptide bond]]
-[[Category: molybdenum cofactor biosynthesis]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:02:22 2007''