8upi

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Current revision (06:00, 5 June 2024) (edit) (undo)
 
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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=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>
<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>
</table>
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== Function ==
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8upi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of a periplasmic peptide binding protein from Mesorhizobium sp. AP09 bound to aminoserine

PDB ID 8upi

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