7c9m
From Proteopedia
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==The structure of product-bound CntL, an aminobutyrate transferase in staphylopine biosynthesis== | ==The structure of product-bound CntL, an aminobutyrate transferase in staphylopine biosynthesis== | ||
| - | <StructureSection load='7c9m' size='340' side='right'caption='[[7c9m]]' scene=''> | + | <StructureSection load='7c9m' size='340' side='right'caption='[[7c9m]], [[Resolution|resolution]] 2.70Å' 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=7C9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7c9m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C9M 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=7c9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c9m OCA], [https://pdbe.org/7c9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c9m RCSB], [https://www.ebi.ac.uk/pdbsum/7c9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c9m ProSAT]</span></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]] 2.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FN6:(2S)-2-azanyl-4-[[(2R)-3-(1H-imidazol-4-yl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]butanoic+acid'>FN6</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</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=7c9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c9m OCA], [https://pdbe.org/7c9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c9m RCSB], [https://www.ebi.ac.uk/pdbsum/7c9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c9m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NASLD_STAAM NASLD_STAAM] Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto D-histidine to produce the intermediate (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, cobalt, zinc, copper, and iron, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to staphylococcal virulence (PubMed:27230378, PubMed:29091735). Appears to be specific for D-histidine as substrate (PubMed:29091735).<ref>PMID:27230378</ref> <ref>PMID:29091735</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Staphylopine (StP) and other nicotianamine-like metallophores are crucial for many pathogens to acquire the transition metals from hosts during invasion. CntL from Staphylococcus aureus (SaCntL) catalyzes the condensation of the 2-aminobutyrate (Ab) moiety of S-adenosylmethionine (SAM) with D-histidine in the biosynthesis of StP. Here, we report the crystal structures of SaCntL in complex with either SAM or two products. The structure of SaCntL consists of an N-terminal four-helix bundle (holding catalytic residue E84) and a C-terminal Rossmann fold (binding the substrates). The sequence connecting the N- and C-terminal domains (N-C linker) in SaCntL was found to undergo conformational alternation between open and closed states. Our structural and biochemical analyses suggested that this intrinsically dynamic interdomain linker forms an additional structural module that plays essential roles in ligand diffusion, recognition, and catalysis. We confirmed that SaCntL stereoselectively carries out the catalysis of D-His but not its enantiomer, L-His, and we found that the N-C linker and active site of SaCntL could accommodate both enantiomers. SaCntL is likely able to bind L-His without catalysis, and as a result, L-His could show inhibitory effects toward SaCntL. These findings provide critical structural and mechanistic insights into CntL, which facilitates a better understanding of the biosynthesis of nicotianamine-like metallophores and the discovery of inhibitors of this process. | ||
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| + | Structural insights into the ligand recognition and catalysis of the key aminobutanoyltransferase CntL in staphylopine biosynthesis.,Luo Z, Luo S, Ju Y, Ding P, Xu J, Gu Q, Zhou H FASEB J. 2021 May;35(5):e21575. doi: 10.1096/fj.202002287RR. PMID:33826776<ref>PMID:33826776</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7c9m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Staphylococcus aureus subsp. aureus Mu50]] | ||
[[Category: Luo Z]] | [[Category: Luo Z]] | ||
[[Category: Zhou H]] | [[Category: Zhou H]] | ||
Revision as of 16:00, 29 November 2023
The structure of product-bound CntL, an aminobutyrate transferase in staphylopine biosynthesis
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