1eks

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(New page: 200px<br /><applet load="1eks" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eks, resolution 2.5&Aring;" /> '''ASP128ALA VARIANT OF ...)
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[[Image:1eks.jpg|left|200px]]<br /><applet load="1eks" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eks, resolution 2.5&Aring;" />
 
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'''ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI'''<br />
 
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==Overview==
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==ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI==
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BACKGROUND: The molybdenum cofactor (Moco) is an essential component of a, large family of enzymes involved in important transformations in carbon, nitrogen and sulfur metabolism. The Moco biosynthetic pathway is, evolutionarily conserved and found in archaea, eubacteria and eukaryotes., In humans, genetic deficiencies of enzymes involved in this pathway, trigger an autosomal recessive and usually deadly disease with severe, neurological symptoms. The MoaC protein, together with the MoaA protein, is involved in the first step of Moco biosynthesis. RESULTS: MoaC from, Escherichia coli has been expressed and purified to homogeneity and its, crystal structure determined at 2 A resolution. The enzyme is organized, into a tightly packed hexamer with 32 symmetry. The monomer consists of an, antiparallel, four-stranded beta sheet packed against two long alpha, helices, and its fold belongs to the ferredoxin-like family. Analysis of, structural and biochemical data strongly suggests that the active site is, located at the interface of two monomers in a pocket that contains several, strictly conserved residues. CONCLUSIONS: Asp128 in the putative active, site appears to be important for catalysis as its replacement with alanine, almost completely abolishes protein activity. The structure of the, Asp128--&gt;Ala variant reveals substantial conformational changes in an, adjacent loop. In the human MoaC ortholog, substitution of Thr182 with, proline causes Moco deficiency, and the corresponding substitution in MoaC, severely compromises activity. This residue is located near the N-terminal, end of helix alpha4 at an interface between two monomers. The MoaC, structure provides a framework for the analysis of additional, dysfunctional mutations in the corresponding human gene.
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<StructureSection load='1eks' size='340' side='right'caption='[[1eks]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1eks]] is a 1 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=1EKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
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1EKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [https://pdbe.org/1eks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [https://www.ebi.ac.uk/pdbsum/1eks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eks ProSAT]</span></td></tr>
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Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC., Wuebbens MM, Liu MT, Rajagopalan K, Schindelin H, Structure. 2000 Jul 15;8(7):709-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903949 10903949]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MOAC_ECOLI MOAC_ECOLI] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).[HAMAP-Rule:MF_01224_B]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/1eks_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eks ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Liu, M.T.W.]]
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[[Category: Liu MTW]]
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[[Category: Rajagopalan, K.V.]]
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[[Category: Rajagopalan KV]]
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[[Category: Schindelin, H.]]
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[[Category: Schindelin H]]
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[[Category: Wuebbens, M.M.]]
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[[Category: Wuebbens MM]]
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[[Category: TLA]]
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[[Category: moac]]
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[[Category: moco biosynthesis]]
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[[Category: moco deficiency]]
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[[Category: molybdenum cofactor (moco)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:05:25 2007''
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Current revision

ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI

PDB ID 1eks

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