1di6: Difference between revisions

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==1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI==
==1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI==
<StructureSection load='1di6' size='340' side='right' caption='[[1di6]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
<StructureSection load='1di6' size='340' side='right'caption='[[1di6]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1di6]] is a 1 chain structure with sequence 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=1DI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DI6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1di6]] 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=1DI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DI6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1di6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1di6 RCSB], [http://www.ebi.ac.uk/pdbsum/1di6 PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1di6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di6 OCA], [https://pdbe.org/1di6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1di6 RCSB], [https://www.ebi.ac.uk/pdbsum/1di6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1di6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOG_ECOLI MOG_ECOLI] Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.<ref>PMID:15632135</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1di6_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1di6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1di6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in archaea, eubacteria, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in this biosynthetic pathway trigger an autosomal recessive disease with severe neurological symptoms, which usually leads to death in early childhood. The MogA protein exhibits affinity for molybdopterin, the organic component of Moco, and has been proposed to act as a molybdochelatase incorporating molybdenum into Moco. MogA is related to the protein gephyrin, which, in addition to its role in Moco biosynthesis, is also responsible for anchoring glycinergic receptors to the cytoskeleton at inhibitory synapses. The high resolution crystal structure of the Escherichia coli MogA protein has been determined, and it reveals a trimeric arrangement in which each monomer contains a central, mostly parallel beta-sheet surrounded by alpha-helices on either side. Based on structural and biochemical data, a putative active site was identified, including two residues that are essential for the catalytic mechanism.
Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.,Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H J Biol Chem. 2000 Jan 21;275(3):1814-22. PMID:10636880<ref>PMID:10636880</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Liu, M T.W]]
[[Category: Large Structures]]
[[Category: Rajagopalan, K V]]
[[Category: Liu MTW]]
[[Category: Schindelin, H]]
[[Category: Rajagopalan KV]]
[[Category: Wuebbens, M M]]
[[Category: Schindelin H]]
[[Category: Gephyrin]]
[[Category: Wuebbens MM]]
[[Category: Moco]]
[[Category: Moco biosynthesis]]
[[Category: Moga]]
[[Category: Molybdenum cofactor]]
[[Category: Unknown function]]

Latest revision as of 09:54, 7 February 2024

1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI

Structural highlights

1di6 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.45Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MOG_ECOLI Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Nichols JD, Rajagopalan KV. In vitro molybdenum ligation to molybdopterin using purified components. J Biol Chem. 2005 Mar 4;280(9):7817-22. Epub 2005 Jan 4. PMID:15632135 doi:http://dx.doi.org/10.1074/jbc.M413783200

1di6, resolution 1.45Å

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