2yjp: Difference between revisions
No edit summary |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Crystal structure of the solute receptors for L-cysteine of Neisseria gonorrhoeae== | ||
<StructureSection load='2yjp' size='340' side='right'caption='[[2yjp]], [[Resolution|resolution]] 2.26Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2yjp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YJP 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]] 2.26Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2yjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjp OCA], [https://pdbe.org/2yjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yjp RCSB], [https://www.ebi.ac.uk/pdbsum/2yjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5F5B5_NEIG1 Q5F5B5_NEIG1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ATP-binding cassette (ABC) transporters are integral membrane proteins that carry a variety of substrates across biological membranes at the expense of ATP. The here considered prokaryotic canonical importers consist of three entities: an extracellular solute receptor, two membrane-intrinsic proteins forming a translocation pathway, and two cytoplasmic ATP-binding subunits. The ngo0372-74 and ngo2011-14 gene clusters from the human pathogen Neisseria gonorrhoeae were predicted by sequence homology as ABC transporters for the uptake of cystine and cysteine, respectively, and chosen for structural characterization. The structure of the receptor component Ngo0372 was obtained in a ligand-free "open" conformation and in a "closed" conformation when co-crystallized with l-cystine. Our data provide the first structural information of an l-cystine ABC transporter. Dissociation constants of 21 and 33 nM for l-cystine and l-selenocystine, respectively, were determined by isothermal titration calorimetry. In contrast, l-cystathionine and l-djenkolic acid are weak binders, while no binding was detectable for S-methyl-l-cysteine. Mutational analysis of two residues from the binding pocket, Trp97 and Tyr59, revealed that the latter is crucial for l-cystine binding. The structure of the Ngo2014 receptor was obtained in closed conformation in complex with co-purified l-cysteine. The protein binds l-cysteine with a K(d) of 26 nM. Comparison of the structures of both receptors and analysis of the ligand binding sites shed light on the mode of ligand recognition and provides insight into the tight binding of both substrates. Moreover, since l-cystine limitation leads to reduction in virulence of N. gonorrhoeae, Ngo0372 might be suited as target for an antimicrobial vaccine. | |||
Crystal Structures of Two Solute Receptors for l-Cystine and l-Cysteine, Respectively, of the Human Pathogen Neisseria gonorrhoeae.,Bulut H, Moniot S, Licht A, Scheffel F, Gathmann S, Saenger W, Schneider E J Mol Biol. 2012 Jan 20;415(3):560-72. Epub 2011 Nov 23. PMID:22138345<ref>PMID:22138345</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2yjp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Neisseria gonorrhoeae FA 1090]] | |||
[[Category: Bulut H]] | |||
== | [[Category: Gathmann S]] | ||
< | [[Category: Licht A]] | ||
[[Category: Neisseria gonorrhoeae]] | [[Category: Moniot S]] | ||
[[Category: Bulut | [[Category: Saenger W]] | ||
[[Category: Gathmann | [[Category: Scheffel F]] | ||
[[Category: Licht | [[Category: Schneider E]] | ||
[[Category: Moniot | |||
[[Category: Saenger | |||
[[Category: Scheffel | |||
[[Category: Schneider | |||
Latest revision as of 13:53, 20 December 2023
Crystal structure of the solute receptors for L-cysteine of Neisseria gonorrhoeaeCrystal structure of the solute receptors for L-cysteine of Neisseria gonorrhoeae
Structural highlights
FunctionPublication Abstract from PubMedATP-binding cassette (ABC) transporters are integral membrane proteins that carry a variety of substrates across biological membranes at the expense of ATP. The here considered prokaryotic canonical importers consist of three entities: an extracellular solute receptor, two membrane-intrinsic proteins forming a translocation pathway, and two cytoplasmic ATP-binding subunits. The ngo0372-74 and ngo2011-14 gene clusters from the human pathogen Neisseria gonorrhoeae were predicted by sequence homology as ABC transporters for the uptake of cystine and cysteine, respectively, and chosen for structural characterization. The structure of the receptor component Ngo0372 was obtained in a ligand-free "open" conformation and in a "closed" conformation when co-crystallized with l-cystine. Our data provide the first structural information of an l-cystine ABC transporter. Dissociation constants of 21 and 33 nM for l-cystine and l-selenocystine, respectively, were determined by isothermal titration calorimetry. In contrast, l-cystathionine and l-djenkolic acid are weak binders, while no binding was detectable for S-methyl-l-cysteine. Mutational analysis of two residues from the binding pocket, Trp97 and Tyr59, revealed that the latter is crucial for l-cystine binding. The structure of the Ngo2014 receptor was obtained in closed conformation in complex with co-purified l-cysteine. The protein binds l-cysteine with a K(d) of 26 nM. Comparison of the structures of both receptors and analysis of the ligand binding sites shed light on the mode of ligand recognition and provides insight into the tight binding of both substrates. Moreover, since l-cystine limitation leads to reduction in virulence of N. gonorrhoeae, Ngo0372 might be suited as target for an antimicrobial vaccine. Crystal Structures of Two Solute Receptors for l-Cystine and l-Cysteine, Respectively, of the Human Pathogen Neisseria gonorrhoeae.,Bulut H, Moniot S, Licht A, Scheffel F, Gathmann S, Saenger W, Schneider E J Mol Biol. 2012 Jan 20;415(3):560-72. Epub 2011 Nov 23. PMID:22138345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||