1z6h
From Proteopedia
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| - | [[Image:1z6h.gif|left|200px]] | + | [[Image:1z6h.gif|left|200px]] |
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| - | '''Solution Structure of Bacillus subtilis BLAP biotinylated-form''' | + | {{Structure |
| + | |PDB= 1z6h |SIZE=350|CAPTION= <scene name='initialview01'>1z6h</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of Bacillus subtilis BLAP biotinylated-form''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z6H is a [ | + | 1Z6H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6H OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16699181 16699181] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Xia, B.]] | [[Category: Xia, B.]] | ||
[[Category: BTI]] | [[Category: BTI]] | ||
| - | [[Category: bacillus | + | [[Category: bacillus subtili]] |
[[Category: single-domain biotin/lipoyl attachment protein]] | [[Category: single-domain biotin/lipoyl attachment protein]] | ||
[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:31:43 2008'' |
Revision as of 13:31, 20 March 2008
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Solution Structure of Bacillus subtilis BLAP biotinylated-form
Overview
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.
About this Structure
1Z6H is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 15:31:43 2008
