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4g4p

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==Crystal structure of glutamine-binding protein from Enterococcus faecalis at 1.5 A==
==Crystal structure of glutamine-binding protein from Enterococcus faecalis at 1.5 A==
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<StructureSection load='4g4p' size='340' side='right' caption='[[4g4p]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='4g4p' size='340' side='right'caption='[[4g4p]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g4p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis_v583 Enterococcus faecalis v583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G4P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g4p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis_V583 Enterococcus faecalis V583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G4P 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>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EF_0761 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226185 Enterococcus faecalis V583])</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>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=4g4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g4p RCSB], [http://www.ebi.ac.uk/pdbsum/4g4p PDBsum]</span></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=4g4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4p OCA], [https://pdbe.org/4g4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g4p RCSB], [https://www.ebi.ac.uk/pdbsum/4g4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g4p ProSAT]</span></td></tr>
</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/Q837S0_ENTFA Q837S0_ENTFA]
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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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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterococcus faecalis v583]]
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[[Category: Enterococcus faecalis V583]]
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[[Category: Fulyani, F]]
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[[Category: Large Structures]]
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[[Category: Guskov, A]]
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[[Category: Fulyani F]]
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[[Category: Poolman, B]]
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[[Category: Guskov A]]
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[[Category: Slotboom, D J]]
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[[Category: Poolman B]]
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[[Category: Zagar, A V]]
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[[Category: Slotboom D-J]]
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[[Category: Abc transporter]]
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[[Category: Zagar AV]]
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[[Category: Glutamine/glutamate binding]]
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[[Category: Substrate-binding domain]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of glutamine-binding protein from Enterococcus faecalis at 1.5 A

PDB ID 4g4p

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