4njg
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4njg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_multivorans_ATCC_17616 Burkholderia multivorans ATCC 17616]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NJG FirstGlance]. <br> | <table><tr><td colspan='2'>[[4njg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_multivorans_ATCC_17616 Burkholderia multivorans ATCC 17616]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NJG FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HHS:6-CARBOXYPTERIN'>HHS</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.598Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HHS:6-CARBOXYPTERIN'>HHS</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=4njg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4njg OCA], [https://pdbe.org/4njg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4njg RCSB], [https://www.ebi.ac.uk/pdbsum/4njg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4njg 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=4njg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4njg OCA], [https://pdbe.org/4njg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4njg RCSB], [https://www.ebi.ac.uk/pdbsum/4njg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4njg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/QUEE_BURM1 QUEE_BURM1] 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:24362703</ref> | [https://www.uniprot.org/uniprot/QUEE_BURM1 QUEE_BURM1] 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:24362703</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 7-carboxy-7-deazaguanine synthase (QueE) catalyzes a key S-adenosyl-L-methionine (AdoMet)- and Mg(2+)-dependent radical-mediated ring contraction step, which is common to the biosynthetic pathways of all deazapurine-containing compounds. QueE is a member of the AdoMet radical superfamily, which employs the 5'-deoxyadenosyl radical from reductive cleavage of AdoMet to initiate chemistry. To provide a mechanistic rationale for this elaborate transformation, we present the crystal structure of a QueE along with structures of pre- and post-turnover states. We find that substrate binds perpendicular to the [4Fe-4S]-bound AdoMet, exposing its C6 hydrogen atom for abstraction and generating the binding site for Mg(2+), which coordinates directly to the substrate. The Burkholderia multivorans structure reported here varies from all other previously characterized members of the AdoMet radical superfamily in that it contains a hypermodified (beta6/alpha3) protein core and an expanded cluster-binding motif, CX14CX2C. | ||
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| - | Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.,Dowling DP, Bruender NA, Young AP, McCarty RM, Bandarian V, Drennan CL Nat Chem Biol. 2014 Feb;10(2):106-12. doi: 10.1038/nchembio.1426. Epub 2013 Dec, 22. PMID:24362703<ref>PMID:24362703</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4njg" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure of QueE from Burkholderia multivorans in complex with AdoMet and 6-carboxypterin
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