5yh8: Difference between revisions

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==The crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickel==
==The crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickel==
<StructureSection load='5yh8' size='340' side='right' caption='[[5yh8]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
<StructureSection load='5yh8' size='340' side='right'caption='[[5yh8]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5yh8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YH8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5yh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YH8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8UX:(2~{S})-4-[[(2~{R})-3-(1~{H}-imidazol-4-yl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-2-[[(2~{S})-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]butanoic+acid'>8UX</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.12&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">opp-1A, AYM28_13740, AYM37_13740, ERS072738_00487, ERS074020_00717, HMPREF3211_02361 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8UX:(2~{S})-4-[[(2~{R})-3-(1~{H}-imidazol-4-yl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-2-[[(2~{S})-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]butanoic+acid'>8UX</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<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=5yh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yh8 OCA], [http://pdbe.org/5yh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yh8 RCSB], [http://www.ebi.ac.uk/pdbsum/5yh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yh8 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=5yh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yh8 OCA], [https://pdbe.org/5yh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yh8 RCSB], [https://www.ebi.ac.uk/pdbsum/5yh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yh8 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/CNTA_STAA8 CNTA_STAA8] Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease (PubMed:23279021, PubMed:29581261). Binds one molecule of StP/metal. Binds StP/Co(2+) and StP/Ni(2+) tighter than StP/Zn(2+) (PubMed:29581261). Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro (PubMed:23279021).<ref>PMID:23279021</ref> <ref>PMID:29581261</ref>
Metal acquisition is vital to pathogens for successful infection within hosts. Staphylopine (StP), a broad-spectrum metallophore biosynthesized by the major human pathogen, Staphylococcus aureus, plays a central role in transition-metal acquisition and bacterial virulence. The StP-like biosynthesis loci are present in various pathogens, and the proteins responsible for StP/metal transportation have been determined. However, the molecular mechanisms of how StP/metal complexes are recognized and transported remain unknown. We report multiple structures of the extracytoplasmic solute-binding protein CntA from the StP/metal transportation system in apo form and in complex with StP and three different metals. We elucidated a sophisticated metal-bound StP recognition mechanism and determined that StP/metal binding triggers a notable interdomain conformational change in CntA. Furthermore, CRISPR/Cas9-mediated single-base substitution mutations and biochemical analysis highlight the importance of StP/metal recognition for StP/metal acquisition. These discoveries provide critical insights into the study of novel metal-acquisition mechanisms in microbes.


Mechanistic insights into staphylopine-mediated metal acquisition.,Song L, Zhang Y, Chen W, Gu T, Zhang SY, Ji Q Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1718382115. doi:, 10.1073/pnas.1718382115. PMID:29581261<ref>PMID:29581261</ref>
==See Also==
 
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yh8" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ji, Q]]
[[Category: Large Structures]]
[[Category: Song, L]]
[[Category: Staphylococcus aureus]]
[[Category: Complex]]
[[Category: Ji Q]]
[[Category: Metal binding protein]]
[[Category: Song L]]
[[Category: Receptor]]

Latest revision as of 13:23, 27 March 2024

The crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickelThe crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickel

Structural highlights

5yh8 is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.12Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CNTA_STAA8 Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease (PubMed:23279021, PubMed:29581261). Binds one molecule of StP/metal. Binds StP/Co(2+) and StP/Ni(2+) tighter than StP/Zn(2+) (PubMed:29581261). Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro (PubMed:23279021).[1] [2]

See Also

References

  1. ↑ Remy L, Carrière M, Derré-Bobillot A, Martini C, Sanguinetti M, Borezée-Durant E. The Staphylococcus aureus Opp1 ABC transporter imports nickel and cobalt in zinc-depleted conditions and contributes to virulence. Mol Microbiol. 2013 Feb;87(4):730-43. PMID:23279021 doi:10.1111/mmi.12126
  2. ↑ Song L, Zhang Y, Chen W, Gu T, Zhang SY, Ji Q. Mechanistic insights into staphylopine-mediated metal acquisition. Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1718382115. doi:, 10.1073/pnas.1718382115. PMID:29581261 doi:http://dx.doi.org/10.1073/pnas.1718382115

5yh8, resolution 2.12Å

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