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4mp8

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Staphyloferrin B precursor biosynthetic enzyme SbnB bound to malonate and NAD+

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Retrieved from "http://52.214.119.220/wiki/index.php/4mp8"

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 ==Staphyloferrin B precursor biosynthetic enzyme SbnB bound to malonate and NAD+==
-<StructureSection load='4mp8' size='340' side='right' caption='[[4mp8]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='4mp8' size='340' side='right'caption='[[4mp8]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4mp8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staaw Staaw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MP8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MP8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4mp8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MP8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 1.85&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m54|4m54]], [[4mp3|4mp3]], [[4mp6|4mp6]], [[4mpd|4mpd]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbnB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=196620 STAAW])</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=4mp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mp8 OCA], [https://pdbe.org/4mp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mp8 RCSB], [https://www.ebi.ac.uk/pdbsum/4mp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mp8 ProSAT]</span></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=4mp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mp8 OCA], [http://pdbe.org/4mp8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mp8 RCSB], [http://www.ebi.ac.uk/pdbsum/4mp8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mp8 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A0H3K9Y6_STAAE A0A0H3K9Y6_STAAE]
-L-2,3-diaminopropionic acid (L-Dap) is an amino acid that is a precursor of antibiotics and staphyloferrin B a siderophore produced by Staphylococcus aureus. SbnA and SbnB are encoded by the staphyloferrin B biosynthetic gene cluster and are implicated in L-Dap biosynthesis. We demonstrate here that SbnA uses PLP and substrates O-phospho-L-serine and L-glutamate to produce a metabolite N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid (ACEGA). SbnB is shown to use NAD(+) to oxidatively hydrolyze ACEGA to yield alpha-ketoglutarate and L-Dap. Also, we describe crystal structures of SbnB in complex with NADH and ACEGA as well as with NAD(+) and alpha-ketoglutarate to reveal the residues required for substrate binding, oxidation, and hydrolysis. SbnA and SbnB contribute to the iron sparing response of S. aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle.
-Synthesis of L-2,3-diaminopropionic Acid, a siderophore and antibiotic precursor.,Kobylarz MJ, Grigg JC, Takayama SJ, Rai DK, Heinrichs DE, Murphy ME Chem Biol. 2014 Mar 20;21(3):379-88. doi: 10.1016/j.chembiol.2013.12.011. Epub, 2014 Jan 30. PMID:24485762<ref>PMID:24485762</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4mp8" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Staaw]]
+[[Category: Large Structures]]
-[[Category: Grigg, J C]]
+[[Category: Staphylococcus aureus subsp. aureus MW2]]
-[[Category: Kobylarz, M J]]
+[[Category: Grigg JC]]
-[[Category: Murphy, M E.P]]
+[[Category: Kobylarz MJ]]
-[[Category: Rai, D K]]
+[[Category: Murphy MEP]]
-[[Category: Acega dehydrogenase]]
+[[Category: Rai DK]]
-[[Category: L-dap synthesis]]
-[[Category: Oxidoreductase]]
-[[Category: Siderophore]]

4mp8

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Staphyloferrin B precursor biosynthetic enzyme SbnB bound to malonate and NAD+

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