4la9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4la9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_Il1403 Lactococcus lactis subsp. lactis Il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LA9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4la9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_Il1403 Lactococcus lactis subsp. lactis Il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LA9 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 1.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4la9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4la9 OCA], [https://pdbe.org/4la9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4la9 RCSB], [https://www.ebi.ac.uk/pdbsum/4la9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4la9 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=4la9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4la9 OCA], [https://pdbe.org/4la9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4la9 RCSB], [https://www.ebi.ac.uk/pdbsum/4la9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4la9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9CES5_LACLA Q9CES5_LACLA] | [https://www.uniprot.org/uniprot/Q9CES5_LACLA Q9CES5_LACLA] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The ATP-binding cassette (ABC) transporter GlnPQ is an essential uptake system for amino acids in gram-positive pathogens and related nonpathogenic bacteria. The transporter has tandem substrate-binding domains (SBDs) fused to each transmembrane domain, giving rise to four SBDs per functional transporter complex. We have determined the crystal structures and ligand-binding properties of the SBDs of GlnPQ from Enterococcus faecalis, Streptococcus pneumoniae, and Lactococcus lactis. The tandem SBDs differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. The combined structural, functional, and thermodynamic analysis revealed the roles of individual residues in determining the substrate affinity. We succeeded in converting a low-affinity SBD into a high-affinity receptor and vice versa. Our data indicate that a small number of residues that reside in the binding pocket constitute the major affinity determinants of the SBDs. | ||
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| - | Functional Diversity of Tandem Substrate-Binding Domains in ABC Transporters from Pathogenic Bacteria.,Fulyani F, Schuurman-Wolters GK, Zagar AV, Guskov A, Slotboom DJ, Poolman B Structure. 2013 Aug 28. pii: S0969-2126(13)00270-0. doi:, 10.1016/j.str.2013.07.020. PMID:23994008<ref>PMID:23994008</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4la9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[ABC transporter 3D structures|ABC transporter 3D structures]] | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of an empty substrate binding domain 1 (SBD1) OF ABC TRANSPORTER GLNPQ from lactococcus lactis
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