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| | <StructureSection load='5afs' size='340' side='right'caption='[[5afs]], [[Resolution|resolution]] 2.22Å' scene=''> | | <StructureSection load='5afs' size='340' side='right'caption='[[5afs]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5afs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"candidatus_liberobacter_asiaticum"_jagoueix_et_al._1994 "candidatus liberobacter asiaticum" jagoueix et al. 1994]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5afs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Liberibacter_asiaticus Candidatus Liberibacter asiaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AFS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5afs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afs OCA], [http://pdbe.org/5afs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5afs RCSB], [http://www.ebi.ac.uk/pdbsum/5afs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5afs 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=5afs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afs OCA], [https://pdbe.org/5afs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5afs RCSB], [https://www.ebi.ac.uk/pdbsum/5afs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5afs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C6XF58_LIBAP C6XF58_LIBAP] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candidatus liberobacter asiaticum jagoueix et al. 1994]] | + | [[Category: Candidatus Liberibacter asiaticus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kumar, P]] | + | [[Category: Kumar P]] |
| - | [[Category: Selvakumar, P]] | + | [[Category: Selvakumar P]] |
| - | [[Category: Sharma, A K]] | + | [[Category: Sharma AK]] |
| - | [[Category: Sharma, N]] | + | [[Category: Sharma N]] |
| - | [[Category: Metal ion transporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
C6XF58_LIBAP
Publication Abstract from PubMed
A periplasmic solute binding protein from second of the two gene clusters of Znu system in CLA (CLas-ZnuA2) belong to Cluster A1 family of solute binding proteins (SBPs). The crystal structures in metal-free, intermediate and metal-bound states, in the previous study, revealed the unusual mechanism of metal binding and release for CLas-ZnuA2. Although CLas-ZnuA2 showed maximum sequence identity to the Mn/Fe-specific SBPs, the mechanistic resemblance seems to be closer to Zn-specific SBPs of Cluster A-I family. The present study reports the binding affinity studies using SPR and CD and crystal structure of CLas-ZnuA2 in Zn2+-bound state. Despite a similar overall structure, there are noticeable differences at the metal binding site. The SPR and CD analysis confirmed our previous observation that CLas-ZnuA2 exhibits a low metal-binding affinity. The low metal-binding affinity of CLas-ZnuA2 could be attributed to the presence of a proline in linker helix resulting in relatively higher bending and rigidity of the same. This structural feature fixes the C-domain similar to metal-bound states of related SBPs. Further, the binding of both Mn2+ and Zn2+ occurs pentavalently with square pyramidal geometry not preferred by either. The site-specific positive Darwinian selection analysis showed that the proline in linker helix is under purifying selection and might have diverged long ago. Our structural and evolutionary analyses suggest that CLasZnua2 might have evolved, particularly for plant pathogens, to facilitate transport of both Mn2+ and Zn2+, with reversible binding to Zn2+, unlike other Mn-binding SBPs (PsaA).
Crystal structure analysis in Zn2+-bound state and biophysical characterization of CLas-ZnuA2.,Sharma N, Selvakumar P, Saini G, Warghane A, Ghosh DK, Sharma AK Biochim Biophys Acta. 2016 Dec;1864(12):1649-1657. doi:, 10.1016/j.bbapap.2016.08.016. Epub 2016 Aug 26. PMID:27570147[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sharma N, Selvakumar P, Saini G, Warghane A, Ghosh DK, Sharma AK. Crystal structure analysis in Zn2+-bound state and biophysical characterization of CLas-ZnuA2. Biochim Biophys Acta. 2016 Dec;1864(12):1649-1657. doi:, 10.1016/j.bbapap.2016.08.016. Epub 2016 Aug 26. PMID:27570147 doi:http://dx.doi.org/10.1016/j.bbapap.2016.08.016
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