2isl

<StructureSection load='2isl' size='340' side='right' caption='[[2isl]], [[Resolution|resolution]] 2.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[2isl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_9930 Atcc 9930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ISL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ISL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bluB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 ATCC 9930])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2isl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2isl OCA], [http://pdbe.org/2isl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2isl RCSB], [http://www.ebi.ac.uk/pdbsum/2isl PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/BLUB_RHIME BLUB_RHIME]] Involved in the biosynthesis of cobalamin (vitamin B12). Catalyzes the oxidative fragmentation and contraction of the isoalloxazine heterocycle and the cleavage of the ribityl tail of FMN(2) to form 5,6-dimethylbenzimidazole (DMB) and D-erythrose 4-phosphate (E4P). NAD(P)H is only required initially to reduce FMN and oxygen drives the oxidative fragmentation.<ref>PMID:16537439</ref> <ref>PMID:17377583</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/2isl_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Vitamin B12 (cobalamin) is among the largest known non-polymeric natural products, and the only vitamin synthesized exclusively by microorganisms. The biosynthesis of the lower ligand of vitamin B(12), 5,6-dimethylbenzimidazole (DMB), is poorly understood. Recently, we discovered that a Sinorhizobium meliloti gene, bluB, is necessary for DMB biosynthesis. Here we show that BluB triggers the unprecedented fragmentation and contraction of the bound flavin mononucleotide cofactor and cleavage of the ribityl tail to form DMB and D-erythrose 4-phosphate. Our structural analysis shows that BluB resembles an NAD(P)H-flavin oxidoreductase, except that its unusually tight binding pocket accommodates flavin mononucleotide but not NAD(P)H. We characterize crystallographically an early intermediate along the reaction coordinate, revealing molecular oxygen poised over reduced flavin. Thus, BluB isolates and directs reduced flavin to activate molecular oxygen for its own cannibalization. This investigation of the biosynthesis of DMB provides clarification of an aspect of vitamin B12 that was otherwise incomplete, and may contribute to a better understanding of vitamin B12-related disease.

BluB cannibalizes flavin to form the lower ligand of vitamin B12.,Taga ME, Larsen NA, Howard-Jones AR, Walsh CT, Walker GC Nature. 2007 Mar 22;446(7134):449-53. PMID:17377583<ref>PMID:17377583</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2isl" style="background-color:#fffaf0;"></div>

[[Category: Atcc 9930]]

[[Category: Howard-Jones, A R]]

[[Category: Larsen, N A]]

[[Category: Taga, M E]]

[[Category: Walker, G C]]

[[Category: Walsh, C T]]

[[Category: Oxidoreductase]]