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| | <StructureSection load='4r99' size='340' side='right'caption='[[4r99]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4r99' size='340' side='right'caption='[[4r99]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r99]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29604 Atcc 29604]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R99 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r99]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Metabacillus_fastidiosus Metabacillus fastidiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R99 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r8x|4r8x]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyisobutyryl-CoA_hydrolase 3-hydroxyisobutyryl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.4 3.1.2.4] </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=4r99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r99 OCA], [https://pdbe.org/4r99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r99 RCSB], [https://www.ebi.ac.uk/pdbsum/4r99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r99 ProSAT]</span></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=4r99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r99 OCA], [http://pdbe.org/4r99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r99 RCSB], [http://www.ebi.ac.uk/pdbsum/4r99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r99 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C5HDG5_9BACI C5HDG5_9BACI] |
| | <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: 3-hydroxyisobutyryl-CoA hydrolase]] | |
| - | [[Category: Atcc 29604]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Feng, J]] | + | [[Category: Metabacillus fastidiosus]] |
| - | [[Category: Liao, F]] | + | [[Category: Feng J]] |
| - | [[Category: Liu, H B]] | + | [[Category: Liao F]] |
| - | [[Category: Liu, L]] | + | [[Category: Liu HB]] |
| - | [[Category: Wang, L]] | + | [[Category: Liu L]] |
| - | [[Category: Bacillus fastidious uricase]]
| + | [[Category: Wang L]] |
| - | [[Category: Fold]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Stability]]
| + | |
| Structural highlights
Function
C5HDG5_9BACI
Publication Abstract from PubMed
Bacillus fastidious uricase (BF uricase) containing 322 amino acid residues exhibited high stability under physiological conditions. Its crystal structure was solved to 1.4-A resolution, showing homotetramer containing two homodimers. After the intersubunit antiparallel beta-sheet in its homodimer, each subunit had a total of 18 C-terminus residues forming an alpha-helix (Q305-A313) and random coil (S314-L322) on surface to bury other two alpha-helices (I227-T238 and I244-R258). In comparison, reported crystal structures of Arthrobacter globiformis and Aspergillus flavus uricases had atomic coordinates of only some C-terminus residues, while the crystal structures of all the other uricases accessible before September 2014 missed atomic coordinates of all their C-terminus residues, after the intersubunit antiparallel beta-sheets. In each homodimer of BF uricase, H-bonds were found between E311 and Y249 and between Y319 and D257; electrostatic interaction networks were found to surround D307 plus R310 and intersubunit R3, K312 plus D257, E318 plus K242, and L322 plus R258. Amino acid mutations that disrupted those interactions when R3 and D307 were reserved caused moderate decreases of activity at pH 9.2 while negligible decreases of activity at pH 7.4, but destroyed stability at pH 7.4 while slightly decreased stability at pH 9.2. Such structural information guided the fusion of 6His-tag to the C-terminus of the mutant L322D with SNSNSN as a linker to reserve the activity and stability. Hence, the folding of the C-terminus residues is crucial for thermal stability of BF uricase under physiological conditions; these new structural insights are valuable for molecular engineering of uricases.
Crystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions.,Feng J, Wang L, Liu H, Yang X, Liu L, Xie Y, Liu M, Zhao Y, Li X, Wang D, Zhan CG, Liao F Appl Microbiol Biotechnol. 2015 Mar 20. PMID:25786739[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feng J, Wang L, Liu H, Yang X, Liu L, Xie Y, Liu M, Zhao Y, Li X, Wang D, Zhan CG, Liao F. Crystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions. Appl Microbiol Biotechnol. 2015 Mar 20. PMID:25786739 doi:http://dx.doi.org/10.1007/s00253-015-6520-6
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