2KWL
Solution Structure of acyl carrier protein from Borrelia burgdorferi
Summary for 2KWL
| Entry DOI | 10.2210/pdb2kwl/pdb |
| NMR Information | BMRB: 16856 |
| Descriptor | Acyl carrier protein (1 entity in total) |
| Functional Keywords | acyl carrier protein, structural genomics, seattle structural genomics center for infectious disease, ssgcid, lipid binding protein |
| Biological source | Borrelia burgdorferi (Lyme disease spirochete) |
| Cellular location | Cytoplasm (By similarity): O51647 |
| Total number of polymer chains | 1 |
| Total formula weight | 9642.56 |
| Authors | Barnwal, R.,Vittal, V.,Moody, J.,Varani, G.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-04-12, release date: 2010-04-28, Last modification date: 2024-05-01) |
| Primary citation | Barnwal, R.P.,Van Voorhis, W.C.,Varani, G. NMR structure of an acyl-carrier protein from Borrelia burgdorferi. Acta Crystallogr.,Sect.F, 67:1137-1140, 2011 Cited by PubMed Abstract: Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein was chosen as a potential target for drug-discovery efforts because of its involvement in fatty-acid biosynthesis, an essential metabolic pathway, in bacteria. It was possible to assign >98% of backbone resonances and >92% of side-chain resonances using multidimensional NMR spectroscopy. The NMR structure was determined to a backbone r.m.s.d. of 0.4 Å and contained four α-helices and two 3(10)-helices. A structure-homology search revealed that this protein is highly similar to the acyl-carrier protein from Aquifex aeolicus. PubMed: 21904063DOI: 10.1107/S1744309111004386 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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