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1g8l

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Revision as of 06:45, 3 January 2018

CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA

Structural highlights

1g8l is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1g8r
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MOEA_ECOLI] Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.^[1]

Evolutionary Conservation

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

Publication Abstract from PubMed

BACKGROUND: Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in archaea, eubacteria, and eukaryotes. In humans, genetic abnormalities in the biosynthetic pathway result in Moco deficiency, which is accompanied by severe neurological symptoms and death shortly after birth. The Escherichia coli MoeA and MogA proteins are involved in the final step of Moco biosynthesis: the incorporation of molybdenum into molybdopterin (MPT), the organic pyranopterin moiety of Moco. RESULTS: The crystal structure of E. coli MoeA has been refined at 2 A resolution and reveals that the highly elongated MoeA monomer consists of four clearly separated domains, one of which is structurally related to MogA, indicating a divergent evolutionary relationship between both proteins. The active form of MoeA is a dimer, and a putative active site appears to be localized to a cleft formed between domain II of the first monomer and domains III and IV of the second monomer. CONCLUSIONS: In eukaryotes, MogA and MoeA are fused into a single polypeptide chain. The corresponding mammalian protein gephyrin has also been implicated in the anchoring of glycinergic receptors to the cytoskeleton at inhibitory synapses. Based on the structures of MoeA and MogA, gephyrin is surmised to be a highly organized molecule containing at least five domains. This multidomain arrangement could provide a structural basis for its functional diversity. The oligomeric states of MoeA and MogA suggest how gephyrin could assemble into a hexagonal scaffold at inhibitory synapses.

The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin.,Xiang S, Nichols J, Rajagopalan KV, Schindelin H Structure. 2001 Apr 4;9(4):299-310. PMID:11525167^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Xiang S, Nichols J, Rajagopalan KV, Schindelin H. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure. 2001 Apr 4;9(4):299-310. PMID:11525167

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g8l"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA==
 <StructureSection load='1g8l' size='340' side='right' caption='[[1g8l]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g8r|1g8r]]</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=1g8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8l OCA], [http://pdbe.org/1g8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g8l RCSB], [http://www.ebi.ac.uk/pdbsum/1g8l PDBsum]</span></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=1g8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8l OCA], [http://pdbe.org/1g8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g8l RCSB], [http://www.ebi.ac.uk/pdbsum/1g8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g8l ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g8/1g8l_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g8/1g8l_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1g8l

From Proteopedia

Revision as of 06:45, 3 January 2018

CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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