8upi
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8upi is ON HOLD Authors: Frkic, R.L., Smith, O.B., Rahman, M., Kaczmarski, J.A., Jackson, C.J. Description: Structure of a periplasmic peptide bind...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a periplasmic peptide binding protein from Mesorhizobium sp. AP09 bound to aminoserine== | |
| + | <StructureSection load='8upi' size='340' side='right'caption='[[8upi]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8upi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_sp._AP09 Mesorhizobium sp. AP09]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UPI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SET:AMINOSERINE'>SET</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=8upi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8upi OCA], [https://pdbe.org/8upi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8upi RCSB], [https://www.ebi.ac.uk/pdbsum/8upi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8upi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A7R6WUD2_9HYPH A0A7R6WUD2_9HYPH] Probably part of an ABC transporter complex that could be involved in peptide import.[ARBA:ARBA00037680] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Periplasmic solute-binding proteins (SBPs) are key ligand recognition components of bacterial ATP-binding cassette (ABC) transporters that allow bacteria to import nutrients and metabolic precursors from the environment. Periplasmic SBPs comprise a large and diverse family of proteins, of which only a small number have been empirically characterized. In this work, we identify a set of 610 unique uncharacterized proteins within the SBP_bac_5 family that are found in conserved operons comprising genes encoding (i) ABC transport systems and (ii) putative amidases from the FmdA_AmdA family. From these uncharacterized SBP_bac_5 proteins, we characterize a representative periplasmic SBP from Mesorhizobium sp. A09 (MeAmi_SBP) and show that MeAmi_SBP binds l-amino acid amides but not the corresponding l-amino acids. An X-ray crystal structure of MeAmi_SBP bound to l-serinamide highlights the residues that impart distinct specificity for l-amino acid amides and reveals a structural Ca(2+) binding site within one of the lobes of the protein. We show that the residues involved in ligand and Ca(2+) binding are conserved among the 610 SBPs from experimentally uncharacterized FmdA_AmdA amidase-associated ABC transporter systems, suggesting these homologous systems are also likely to be involved in the sensing, uptake, and metabolism of l-amino acid amides across many Gram-negative nitrogen-fixing soil bacteria. We propose that MeAmi_SBP is involved in the uptake of such solutes to supplement pathways such as the citric acid cycle and the glutamine synthetase-glutamate synthase pathway. This work expands our currently limited understanding of microbial interactions with l-amino acid amides and bacterial nitrogen utilization. | ||
| - | + | Identification and Characterization of a Bacterial Periplasmic Solute Binding Protein That Binds l-Amino Acid Amides.,Smith OB, Frkic RL, Rahman MG, Jackson CJ, Kaczmarski JA Biochemistry. 2024 May 21;63(10):1322-1334. doi: 10.1021/acs.biochem.4c00096. , Epub 2024 May 2. PMID:38696389<ref>PMID:38696389</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8upi" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Kaczmarski | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mesorhizobium sp. AP09]] | ||
| + | [[Category: Frkic RL]] | ||
| + | [[Category: Jackson CJ]] | ||
| + | [[Category: Kaczmarski JA]] | ||
| + | [[Category: Rahman M]] | ||
| + | [[Category: Smith OB]] | ||
Current revision
Structure of a periplasmic peptide binding protein from Mesorhizobium sp. AP09 bound to aminoserine
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