View source for 5th5


==Crystal Structure of QueE from Bacillus subtilis with 6-carboxypterin-5'-deoxyadenosyl ester bound==
<StructureSection load='5th5' size='340' side='right'caption='[[5th5]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5th5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TH5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.407&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7C5:5-O-(2-AMINO-4-OXO-1,4-DIHYDROPTERIDINE-6-CARBONYL)ADENOSINE'>7C5</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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=5th5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5th5 OCA], [https://pdbe.org/5th5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5th5 RCSB], [https://www.ebi.ac.uk/pdbsum/5th5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5th5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/QUEE_BACSU QUEE_BACSU] Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.[HAMAP-Rule:MF_00917]<ref>PMID:14660578</ref> <ref>PMID:19354300</ref> <ref>PMID:23194065</ref> 
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== Publication Abstract from PubMed ==
Radical S-adenosyl-L-methionine (SAM) enzymes are widely distributed and catalyze diverse reactions. SAM binds to the unique iron atom of a site-differentiated [4Fe-4S] cluster and is reductively cleaved to generate a 5-deoxyadenosyl radical, which initiates turnover. 7-Carboxy-7-deazaguanine (CDG) synthase catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products. 6-Carboxypterin (6-CP), an oxidized analog of the natural substrate 6-carboxy-5,6,7,8-tetrahydropterin (CPH4), is shown to be an alternate substrate for CDG synthase. Under reducing conditions that would promote the reductive cleavage of SAM, 6-CP is turned over to 6-deoxyadenosylpterin, presumably by radical addition of the 5-deoxyadenosine followed by oxidative decarboxylation to the product. By contrast, in the absence of the strong reductant, dithionite, the carboxylate of 6-CP is esterified to generate 6-carboxypterin-5-deoxyadenosyl ester. Structural studies with 6-CP and SAM also reveal electron density consistent with the ester product being formed in crystallo. The differential reactivity of 6-CP under reducing and non-reducing conditions highlights the ability of radical SAM enzymes to carry out both polar and radical transformations in the same active site. .

7-Carboxy-7-deazaguanine synthase - A radical S-adenosyl-L-methionine enzyme with polar tendencies.,Bruender NA, Grell TA, Dowling DP, McCarty RM, Drennan CL, Bandarian V J Am Chem Soc. 2017 Jan 3. doi: 10.1021/jacs.6b11381. PMID:28045519<ref>PMID:28045519</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5th5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Dowling DP]]
[[Category: Drennan CL]]
[[Category: Grell TAJ]]