View source for 3zk8


==CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA E205Q IN THE METAL-FREE, OPEN STATE==
<StructureSection load='3zk8' size='340' side='right'caption='[[3zk8]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zk8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZK8 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=3zk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zk8 OCA], [https://pdbe.org/3zk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zk8 RCSB], [https://www.ebi.ac.uk/pdbsum/3zk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zk8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MTSA_STRPN MTSA_STRPN] Part of an ATP-driven transport system for manganese. Also act as an adhesin which is involved on adherence to extracellular matrix. It is an important factor in pathogenesis and infection.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The relative stability of divalent first-row transition metal ion complexes, as defined by the Irving-Williams series, poses a fundamental chemical challenge for selectivity in bacterial metal ion acquisition. Here we show that although the substrate-binding protein of Streptococcus pneumoniae, PsaA, is finely attuned to bind its physiological substrate manganese, it can also bind a broad range of other divalent transition metal cations. By combining high-resolution structural data, metal-binding assays and mutational analyses, we show that the inability of open-state PsaA to satisfy the preferred coordination chemistry of manganese enables the protein to undergo the conformational changes required for cargo release to the Psa permease. This is specific for manganese ions, whereas zinc ions remain bound to PsaA. Collectively, these findings suggest a new ligand binding and release mechanism for PsaA and related substrate-binding proteins that facilitate specificity for divalent cations during competition from zinc ions, which are more abundant in biological systems.

Imperfect coordination chemistry facilitates metal ion release in the Psa permease.,Counago RM, Ween MP, Begg SL, Bajaj M, Zuegg J, O'Mara ML, Cooper MA, McEwan AG, Paton JC, Kobe B, McDevitt CA Nat Chem Biol. 2013 Nov 10. doi: 10.1038/nchembio.1382. PMID:24212134<ref>PMID:24212134</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zk8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Bajaj M]]
[[Category: Cooper MA]]
[[Category: Counago RM]]
[[Category: Kobe B]]
[[Category: McDevitt CA]]
[[Category: McEwan AG]]
[[Category: Paton JC]]
[[Category: Ween MP]]
[[Category: Zuegg J]]