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==Crystal structure of KabA from Bacillus cereus UW85 in complex with the internal aldimine==
==Crystal structure of KabA from Bacillus cereus UW85 in complex with the internal aldimine==
<StructureSection load='7kz3' size='340' side='right'caption='[[7kz3]]' scene=''>
<StructureSection load='7kz3' size='340' side='right'caption='[[7kz3]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KZ3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7kz3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KZ3 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=7kz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz3 OCA], [https://pdbe.org/7kz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kz3 RCSB], [https://www.ebi.ac.uk/pdbsum/7kz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz3 ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kabA, GE376_30835 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=7kz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz3 OCA], [https://pdbe.org/7kz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kz3 RCSB], [https://www.ebi.ac.uk/pdbsum/7kz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz3 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kanosamine is an antibiotic and antifungal monosaccharide. The kanosamine biosynthetic pathway from glucose 6-phosphate in Bacillus cereus UW85 was recently reported, and the functions of each of the three enzymes in the pathway, KabA, KabB and KabC, were demonstrated. KabA, a member of a subclass of the VIbeta family of PLP-dependent aminotransferases, catalyzes the second step in the pathway, generating kanosamine 6-phosphate (K6P) using l-glutamate as the amino-donor. KabA catalysis was shown to be extremely efficient, with a second-order rate constant with respect to K6P transamination of over 10(7) M(-1)s(-1). Here we report the high-resolution structure of KabA in both the PLP- and PMP-bound forms. In addition, co-crystallization with K6P allowed the structure of KabA in complex with the covalent PLP-K6P adduct to be solved. Co-crystallization or soaking with glutamate or 2-oxoglutarate did not result in crystals with either substrate/product. Reduction of the PLP-KabA complex with sodium cyanoborohydride gave an inactivated enzyme, and crystals of the reduced KabA were soaked with the l-glutamate analog glutarate to mimic the KabA-PLP-l-glutamate complex. Together these four structures give a complete picture of how the active site of KabA recognizes substrates for each half-reaction. The KabA structure is discussed in the context of homologous aminotransferases.
Snapshots along the catalytic path of KabA, a PLP-dependent aminotransferase required for kanosamine biosynthesis in Bacillus cereus UW85.,Prasertanan T, Palmer DRJ, Sanders DAR J Struct Biol. 2021 May 11;213(2):107744. doi: 10.1016/j.jsb.2021.107744. PMID:33984505<ref>PMID:33984505</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kz3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspartate transaminase]]
[[Category: Atcc 14579]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Palmer DRJ]]
[[Category: Palmer, D R.J]]
[[Category: Prasertanan T]]
[[Category: Prasertanan, T]]
[[Category: Sanders DAR]]
[[Category: Sanders, D A.R]]
[[Category: Aminotransferase]]
[[Category: Biosynthesis]]
[[Category: Biosynthetic protein]]
[[Category: Kaba]]
[[Category: Kanosamine]]
[[Category: Transferase]]
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