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4kqp

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==Crystal structure of Lactococcus lactis GlnP substrate binding domain 2 (SBD2) in complex with glutamine at 0.95 A resolution==
==Crystal structure of Lactococcus lactis GlnP substrate binding domain 2 (SBD2) in complex with glutamine at 0.95 A resolution==
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<StructureSection load='4kqp' size='340' side='right' caption='[[4kqp]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
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<StructureSection load='4kqp' size='340' side='right'caption='[[4kqp]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4kqp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacla Lacla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KQP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4kqp]] is a 1 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=4KQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KQP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene></td></tr>
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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]] 0.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kr5|4kr5]], [[4kpt|4kpt]]</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=GLN:GLUTAMINE'>GLN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glnP, L165, LL1759 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272623 LACLA])</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=4kqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kqp OCA], [https://pdbe.org/4kqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kqp RCSB], [https://www.ebi.ac.uk/pdbsum/4kqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kqp ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kqp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kqp RCSB], [http://www.ebi.ac.uk/pdbsum/4kqp PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9CES5_LACLA Q9CES5_LACLA]
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lacla]]
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[[Category: Lactococcus lactis subsp. lactis Il1403]]
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[[Category: Guskov, A]]
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[[Category: Large Structures]]
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[[Category: Poolman, B]]
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[[Category: Guskov A]]
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[[Category: Schuurman-Wolters, G K]]
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[[Category: Poolman B]]
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[[Category: Slotboom, D J]]
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[[Category: Schuurman-Wolters GK]]
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[[Category: Zagar, A Vujicic]]
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[[Category: Slotboom DJ]]
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[[Category: Amino acid transport]]
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[[Category: Vujicic Zagar A]]
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[[Category: Extracellular]]
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[[Category: Glutamine/glutamic acid binding]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of Lactococcus lactis GlnP substrate binding domain 2 (SBD2) in complex with glutamine at 0.95 A resolution

PDB ID 4kqp

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