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| | <StructureSection load='4wh0' size='340' side='right'caption='[[4wh0]], [[Resolution|resolution]] 2.56Å' scene=''> | | <StructureSection load='4wh0' size='340' side='right'caption='[[4wh0]], [[Resolution|resolution]] 2.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wh0]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WH0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wh0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WH0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4wh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wh0 OCA], [https://pdbe.org/4wh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wh0 RCSB], [https://www.ebi.ac.uk/pdbsum/4wh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wh0 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wgf|4wgf]]</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=4wh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wh0 OCA], [http://pdbe.org/4wh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4wh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wh0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9I4D6_PSEAE Q9I4D6_PSEAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Pseudomonas aeruginosa]] | | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Denny, P W]] | + | [[Category: Denny PW]] |
| - | [[Category: Groftehauge, M K]] | + | [[Category: Groftehauge MK]] |
| - | [[Category: Pohl, E]] | + | [[Category: Pohl E]] |
| - | [[Category: Truan, D]] | + | [[Category: Truan D]] |
| - | [[Category: Vasil, A]] | + | [[Category: Vasil A]] |
| - | [[Category: Vasil, M L]] | + | [[Category: Vasil ML]] |
| - | [[Category: Co-purified]]
| + | |
| - | [[Category: Contaminant]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Parallel beta-sheet]]
| + | |
| Structural highlights
Function
Q9I4D6_PSEAE
Publication Abstract from PubMed
As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34 and 2.56 A without a priori knowledge of the protein identity or experimental phases. The three-dimensional structure of YcaC adopts a well-known cysteine hydrolase fold with the putative active site residues conserved. The active site cysteine is covalently bound to propionamide in one crystal form, whereas the second form contains an S-mercaptocysteine. The precise biological function of YcaC is unknown; however, related prokaryotic proteins have functions in antibacterial resistance, siderophore production and NADH biosynthesis. Here, we show that YcaC is exceptionally well conserved across both bacterial and fungal species despite being non-ubiquitous. This suggests that whilst YcaC may not be part of an integral pathway, the function could confer a significant evolutionary advantage to microbial life.
Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct.,Groftehauge MK, Truan D, Vasil A, Denny PW, Vasil ML, Pohl E Int J Mol Sci. 2015 Jul 14;16(7):15971-84. doi: 10.3390/ijms160715971. PMID:26184183[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Groftehauge MK, Truan D, Vasil A, Denny PW, Vasil ML, Pohl E. Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct. Int J Mol Sci. 2015 Jul 14;16(7):15971-84. doi: 10.3390/ijms160715971. PMID:26184183 doi:http://dx.doi.org/10.3390/ijms160715971
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