1fma: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fma.gif|left|200px]]
- {{Structure
+==MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)==
-|PDB= 1fma |SIZE=350|CAPTION= <scene name='initialview01'>1fma</scene>, resolution 1.58&Aring;
+<StructureSection load='1fma' size='340' side='right'caption='[[1fma]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE=
+<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>
-}}
+<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>
+</table>
-'''MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)'''
+== 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 ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-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.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fma_consurf.spt"</scriptWhenChecked>
-FMA is a [[Protein complex]] structure of sequences from [http://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].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-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://www.ncbi.nlm.nih.gov/pubmed/11135669 11135669]
+</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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:10:56 2008''