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| | <StructureSection load='2nqq' size='340' side='right'caption='[[2nqq]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2nqq' size='340' side='right'caption='[[2nqq]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nqq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NQQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nqq]] is a 4 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=2NQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NQQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g8r|1g8r]], [[1g8l|1g8l]], [[1fc5|1fc5]], [[1uz5|1uz5]], [[1wu2|1wu2]], [[2nqk|2nqk]], [[2nqm|2nqm]], [[2nqn|2nqn]], [[2nqr|2nqr]], [[2nqs|2nqs]], [[2nqu|2nqu]], [[2nqv|2nqv]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">moeA, bisB, chlE, narE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2nqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nqq OCA], [https://pdbe.org/2nqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nqq RCSB], [https://www.ebi.ac.uk/pdbsum/2nqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nqq ProSAT]</span></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=2nqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nqq OCA], [https://pdbe.org/2nqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nqq RCSB], [https://www.ebi.ac.uk/pdbsum/2nqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nqq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MOEA_ECOLI MOEA_ECOLI]] Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.<ref>PMID:15632135</ref>
| + | [https://www.uniprot.org/uniprot/MOEA_ECOLI MOEA_ECOLI] Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.<ref>PMID:15632135</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nicolas, J]] | + | [[Category: Nicolas J]] |
| - | [[Category: Rajagopalan, K V]] | + | [[Category: Rajagopalan KV]] |
| - | [[Category: Schindelin, H]] | + | [[Category: Schindelin H]] |
| - | [[Category: Xiang, S]] | + | [[Category: Xiang S]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Cinnamon]]
| + | |
| - | [[Category: Cnx1]]
| + | |
| - | [[Category: Gephyrin]]
| + | |
| - | [[Category: Moco]]
| + | |
| - | [[Category: Moea]]
| + | |
| - | [[Category: Moga]]
| + | |
| - | [[Category: Molybdenum]]
| + | |
| - | [[Category: Molybdopterin]]
| + | |
| - | [[Category: Mpt]]
| + | |
| Structural highlights
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
The molybdenum cofactor is ubiquitous in nature, and the pathway for Moco biosynthesis is conserved in all three domains of life. Recent work has helped to illuminate one of the most enigmatic steps in Moco biosynthesis, ligation of metal to molybdopterin (the organic component of the cofactor) to form the active cofactor. In Escherichia coli, the MoeA protein mediates ligation of Mo to molybdopterin while the MogA protein enhances this process in an ATP-dependent manner. The X-ray crystal structures for both proteins have been previously described as well as two essential MogA residues, Asp49 and Asp82. Here we describe a detailed mutational analysis of the MoeA protein. Variants of conserved residues at the putative active site of MoeA were analyzed for a loss of function in two different, previously described assays, one employing moeA- crude extracts and the other utilizing a defined system. Oddly, no correlation was observed between the activity in the two assays. In fact, our results showed a general trend toward an inverse relationship between the activity in each assay. Moco binding studies indicated a strong correlation between a variant's ability to bind Moco and its activity in the purified component assay. Crystal structures of the functionally characterized MoeA variants revealed no major structural changes, indicating that the functional differences observed are not due to disruption of the protein structure. On the basis of these results, two different functional areas were assigned to regions at or near the MoeA active site cleft.
Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft.,Nichols JD, Xiang S, Schindelin H, Rajagopalan KV Biochemistry. 2007 Jan 9;46(1):78-86. PMID:17198377[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
- ↑ Nichols JD, Xiang S, Schindelin H, Rajagopalan KV. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. Biochemistry. 2007 Jan 9;46(1):78-86. PMID:17198377 doi:10.1021/bi061551q
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