4hdr
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hdr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sporomusa_ovata Sporomusa ovata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HDR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hdr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sporomusa_ovata Sporomusa ovata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HDR FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMD:5,6-DIMETHYLBENZIMIDAZOLE'>DMD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.45Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMD:5,6-DIMETHYLBENZIMIDAZOLE'>DMD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4hdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hdr OCA], [https://pdbe.org/4hdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hdr RCSB], [https://www.ebi.ac.uk/pdbsum/4hdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hdr 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=4hdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hdr OCA], [https://pdbe.org/4hdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hdr RCSB], [https://www.ebi.ac.uk/pdbsum/4hdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hdr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/F6MZ55_9FIRM F6MZ55_9FIRM] Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).[SAAS:SAAS00013329] | [https://www.uniprot.org/uniprot/F6MZ55_9FIRM F6MZ55_9FIRM] Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).[SAAS:SAAS00013329] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cobamides (Cbas) are cobalt (Co) containing tetrapyrrole-derivatives involved in enzyme-catalyzed carbon skeleton rearrangements, methyl-group transfers, and reductive dehalogenation. The biosynthesis of cobamides is complex and is only performed by some bacteria and achaea. Cobamides have an upper (Cobeta) ligand (5'-deoxyadenosyl or methyl) and a lower (Coalpha) ligand base that contribute to the axial Co coordinations. The identity of the lower Coalpha ligand varies depending on the organism synthesizing the Cbas. The homoacetogenic bacterium Sporomusa ovata synthesizes two unique phenolic cobamides (i.e., Coalpha-(phenolyl/p-cresolyl)cobamide), which are used in the catabolism of methanol and 3,4-dimethoxybenzoate by this bacterium. The S. ovata ArsAB enzyme activates a phenolic lower ligand prior to its incorporation into the cobamide. ArsAB consists of two subunits, both of which are homologous ( approximately 35% identity) to the well-characterized Salmonella enterica CobT enzyme, which transfers nitrogenous bases such as 5,6-dimethylbenzimidazole (DMB) and adenine, but cannot utilize phenolics. Here we report the three-dimensional structure of ArsAB, which shows that the enzyme forms a pseudosymmetric heterodimer, provide evidence that only the ArsA subunit has base:phosphoribosyl-transferase activity, and propose a mechanism by which phenolic transfer is facilitated by an activated water molecule. | ||
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| - | Structural Insights into the Function of the Nicotinate Mononucleotide:phenol/p-cresol Phosphoribosyltransferase (ArsAB) Enzyme from Sporomusa ovata.,Newmister SA, Chan CH, Escalante-Semerena JC, Rayment I Biochemistry. 2012 Oct 15. PMID:23039029<ref>PMID:23039029</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4hdr" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure of ArsAB in Complex with 5,6-dimethylbenzimidazole
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