4hdn
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hdn]] is a 2 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=4HDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HDN FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hdn]] is a 2 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=4HDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HDN FirstGlance]. <br> | ||
- | </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=4hdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hdn OCA], [https://pdbe.org/4hdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hdn RCSB], [https://www.ebi.ac.uk/pdbsum/4hdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hdn ProSAT]</span></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]] 2.24Å</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=4hdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hdn OCA], [https://pdbe.org/4hdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hdn RCSB], [https://www.ebi.ac.uk/pdbsum/4hdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hdn 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 4hdn" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Crystal Structure of ArsAB in the Substrate-Free State.
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