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| | ==Solution Structure of Bacillus subtilis BLAP biotinylated-form== | | ==Solution Structure of Bacillus subtilis BLAP biotinylated-form== |
| - | <StructureSection load='1z6h' size='340' side='right'caption='[[1z6h]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1z6h' size='340' side='right'caption='[[1z6h]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1z6h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z6H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z6h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z6H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1z6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z6h OCA], [http://pdbe.org/1z6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z6h RCSB], [http://www.ebi.ac.uk/pdbsum/1z6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z6h ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</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=1z6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z6h OCA], [https://pdbe.org/1z6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z6h RCSB], [https://www.ebi.ac.uk/pdbsum/1z6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z6h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BLAP_BACSU BLAP_BACSU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cui, G]] | + | [[Category: Cui G]] |
| - | [[Category: Xia, B]] | + | [[Category: Xia B]] |
| - | [[Category: Bacillus subtili]]
| + | |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Single-domain biotin/lipoyl attachment protein]]
| + | |
| - | [[Category: Solution structure]]
| + | |
| Structural highlights
Function
BLAP_BACSU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein biotinylation and lipoylation are post-translational modifications, in which biotin or lipoic acid is covalently attached to specific proteins containing biotin/lipoyl attachment domains. All the currently reported natural proteins containing biotin/lipoyl attachment domains are multidomain proteins and can only be modified by either biotin or lipoic acid in vivo. We have identified a single domain protein with 73 amino acid residues from Bacillus subtilis strain 168, and it can be both biotinylated and lipoylated in Escherichia coli. The protein is therefore named as biotin/lipoyl attachment protein (BLAP). This is the first report that a natural single domain protein exists as both a biotin and lipoic acid receptor. The solution structure of apo-BLAP showed that it adopts a typical fold of biotin/lipoyl attachment domain. The structure of biotinylated BLAP revealed that the biotin moiety is covalently attached to the side chain of Lys(35), and the bicyclic ring of biotin is folded back and immobilized on the protein surface. The biotin moiety immobilization is mainly due to an interaction between the biotin ureido ring and the indole ring of Trp(12). NMR study also indicated that the lipoyl group of the lipoylated BLAP is also immobilized on the protein surface in a similar fashion as the biotin moiety in the biotinylated protein.
Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis.,Cui G, Nan B, Hu J, Wang Y, Jin C, Xia B J Biol Chem. 2006 Jul 21;281(29):20598-607. Epub 2006 May 14. PMID:16699181[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cui G, Nan B, Hu J, Wang Y, Jin C, Xia B. Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis. J Biol Chem. 2006 Jul 21;281(29):20598-607. Epub 2006 May 14. PMID:16699181 doi:10.1074/jbc.M602660200
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