8if7

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Current revision (12:40, 26 July 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8if7 is ON HOLD until Paper Publication
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==Crystal structure of CmnB==
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<StructureSection load='8if7' size='340' side='right'caption='[[8if7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8if7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharothrix_mutabilis_subsp._capreolus Saccharothrix mutabilis subsp. capreolus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IF7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P1T:2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC+ACID'>P1T</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8if7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8if7 OCA], [https://pdbe.org/8if7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8if7 RCSB], [https://www.ebi.ac.uk/pdbsum/8if7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8if7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A6YEH3_STRMP A6YEH3_STRMP]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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L-2,3-Diaminopropionic acid (L-Dap) is a nonproteinogenic amino acid that plays as an important role as a building block in the biosynthesis of several natural products, including capreomycin, viomycin, zwittermicin, staphyloferrin and dapdiamide. A previous study reported that CmnB and CmnK are two enzymes that are involved in the formation of L-Dap in the biosynthesis of capreomycin. CmnB catalyzes the condensation reaction of O-phospho-L-serine and L-glutamic acid to generate N-(1-amino-1-carboxyl-2-ethyl)glutamic acid, which subsequently undergoes oxidative hydrolysis via CmnK to generate the product L-Dap. Here, the crystal structure of CmnB in complex with the reaction intermediate PLP-alpha-aminoacrylate is reported at 2.2 A resolution. Notably, CmnB is the second known example of a PLP-dependent enzyme that forms a monomeric structure in crystal packing. The crystal structure of CmnB also provides insights into the catalytic mechanism of the enzyme and supports the biosynthetic pathway of L-Dap reported in previous studies.
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Authors: Chang, C.Y., Toh, S.I., Lo, C.L.
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Crystal structure of CmnB involved in the biosynthesis of the nonproteinogenic amino acid L-2,3-diaminopropionic acid.,Toh SI, Lo CL, Chang CY Acta Crystallogr F Struct Biol Commun. 2023 Jul 1;79(Pt 7):193-199. doi: , 10.1107/S2053230X23005769. Epub 2023 Jul 5. PMID:37405487<ref>PMID:37405487</ref>
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Description: Crystal structure of CmnB
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Chang, C.Y]]
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<div class="pdbe-citations 8if7" style="background-color:#fffaf0;"></div>
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[[Category: Lo, C.L]]
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== References ==
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[[Category: Toh, S.I]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharothrix mutabilis subsp. capreolus]]
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[[Category: Chang CY]]
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[[Category: Lo CL]]
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[[Category: Toh SI]]

Current revision

Crystal structure of CmnB

PDB ID 8if7

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